DB code: D00101

RLCP classification 6.30.97700.5320 : Double-bonded atom exchange
8.211.591510.5526 : Isomerization
6.20.85200.5520 : Double-bonded atom exchange
6.10.82600.5900 : Double-bonded atom exchange
8.211.591510.5527 : Isomerization
6.40.521000.5530 : Double-bonded atom exchange
CATH domain 3.90.1150.10 : Aspartate Aminotransferase, domain 1
3.40.640.10 : Aspartate Aminotransferase; domain 2 Catalytic domain
E.C. 2.6.1.1
CSA 1aam 2aat
M-CSA 1aam 2aat
MACiE

CATH domain Related DB codes (homologues)
3.40.640.10 : Aspartate Aminotransferase; domain 2 D00085 D00092 D00102 D00103 D00104 D00107 D00108 D00109 D00255 D00257 D00258 D00265 D00269 D00515 M00031 D00279
3.90.1150.10 : Aspartate Aminotransferase, domain 1 D00085 D00092 D00102 D00103 D00104 D00107 D00108 D00109 D00255 D00257 D00258 D00265 D00269 D00515 M00031 D00279

Uniprot Enzyme Name
UniprotKB Protein name Synonyms RefSeq Pfam
P00503 Aspartate aminotransferase, cytoplasmic
cAspAT
EC 2.6.1.1
EC 2.6.1.3
Cysteine aminotransferase, cytoplasmic
Cysteine transaminase, cytoplasmic
cCAT
Glutamate oxaloacetate transaminase 1
Transaminase A
NP_999092.1 (Protein)
NM_213927.1 (DNA/RNA sequence)
PF00155 (Aminotran_1_2)
[Graphical View]
P00504 Aspartate aminotransferase, cytoplasmic
cAspAT
EC 2.6.1.1
EC 2.6.1.3
Cysteine aminotransferase, cytoplasmic
Cysteine transaminase, cytoplasmic
cCAT
Glutamate oxaloacetate transaminase 1
Transaminase A
NP_990652.1 (Protein)
NM_205321.1 (DNA/RNA sequence)
PF00155 (Aminotran_1_2)
[Graphical View]
P00508 Aspartate aminotransferase, mitochondrial
mAspAT
EC 2.6.1.1
EC 2.6.1.7
Glutamate oxaloacetate transaminase 2
Kynurenine aminotransferase 4
Kynurenine aminotransferase IV
Kynurenine--oxoglutarate transaminase 4
Kynurenine--oxoglutarate transaminase IV
Transaminase A
NP_990854.1 (Protein)
NM_205523.1 (DNA/RNA sequence)
PF00155 (Aminotran_1_2)
[Graphical View]
P00509 Aspartate aminotransferase
AspAT
EC 2.6.1.1
Transaminase A
NP_415448.1 (Protein)
NC_000913.2 (DNA/RNA sequence)
YP_489200.1 (Protein)
NC_007779.1 (DNA/RNA sequence)
PF00155 (Aminotran_1_2)
[Graphical View]
P23542 Aspartate aminotransferase, cytoplasmic
EC 2.6.1.1
Transaminase A
NP_013127.2 (Protein)
NM_001181914.1 (DNA/RNA sequence)
PF00155 (Aminotran_1_2)
[Graphical View]
Q56232 Aspartate aminotransferase
AspAT
EC 2.6.1.1
Transaminase A
YP_143312.1 (Protein)
NC_006461.1 (DNA/RNA sequence)
PF00155 (Aminotran_1_2)
[Graphical View]

KEGG enzyme name
aspartate transaminase
glutamic-oxaloacetic transaminase
glutamic-aspartic transaminase
transaminase A
AAT
AspT
2-oxoglutarate-glutamate aminotransferase
aspartate alpha-ketoglutarate transaminase
aspartate aminotransferase
aspartate-2-oxoglutarate transaminase
aspartic acid aminotransferase
aspartic aminotransferase
aspartyl aminotransferase
AST
glutamate-oxalacetate aminotransferase
glutamate-oxalate transaminase
glutamic-aspartic aminotransferase
glutamic-oxalacetic transaminase
glutamic oxalic transaminase
GOT (enzyme)
L-aspartate transaminase
L-aspartate-alpha-ketoglutarate transaminase
L-aspartate-2-ketoglutarate aminotransferase
L-aspartate-2-oxoglutarate aminotransferase
L-aspartate-2-oxoglutarate-transaminase
L-aspartic aminotransferase
oxaloacetate-aspartate aminotransferase
oxaloacetate transferase
aspartate:2-oxoglutarate aminotransferase
glutamate oxaloacetate transaminase

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P00503 AATC_PIG L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate. Homodimer. Cytoplasm. Pyridoxal phosphate.
P00504 AATC_CHICK L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate. Homodimer. Cytoplasm. Pyridoxal phosphate.
P00508 AATM_CHICK L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate. Homodimer. Mitochondrion matrix. Pyridoxal phosphate.
P00509 AAT_ECOLI L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate. Homodimer. Cytoplasm. Pyridoxal phosphate.
P23542 AATC_YEAST L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate. Homodimer. Cytoplasm. Peroxisome. Note=Targeted to peroxisomes in cells grown in oleate. Pyridoxal phosphate.
Q56232 AAT_THET8 L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate. Homodimer. Cytoplasm (By similarity). Pyridoxal phosphate.

KEGG Pathways
Map code Pathways E.C.
MAP00251 Glutamate metabolism
MAP00252 Alanine and aspartate metabolism
MAP00272 Cysteine metabolism
MAP00330 Arginine and proline metabolism
MAP00350 Tyrosine metabolism
MAP00360 Phenylalanine metabolism
MAP00400 Phenylalanine, tyrosine and tryptophan biosynthesis
MAP00401 Novobiocin biosynthesis
MAP00710 Carbon fixation in photosynthetic organisms
MAP00950 Alkaloid biosynthesis I

Compound table
Cofactors Substrates Products Intermediates
KEGG-id C00018 C00026 C00049 C00025 C00036 I00004 I00034 I00005 C00647 I00006 I00033 I00007
E.C. (carbinolabine)
Compound Pyridoxal phosphate 2-Oxoglutarate L-Aspartate L-Glutamate Oxaloacetate External aldimine intermediate (initial stage:PLP-Asp) Quinonoid intermediate-1 (PLP-Asp) Ketimine intermediate-1 (PLP-Asp) Tetrahedral intermediate from ketimine to PMP Pyridoxamine phosphate (PMP) Ketimine intermediate-2 (PLP-Glu) Quinonoid intermediate-2 (PLP-Glu) External aldimine intermediate (final stage:PLP-Glu)
Type aromatic ring (with nitrogen atoms),phosphate group/phosphate ion carbohydrate,carboxyl group amino acids,carboxyl group amino acids,carboxyl group carbohydrate,carboxyl group
ChEBI 18405
 18405
 		30915
 30915
 		17053
 17053
 		16015
 16015
 		30744
 30744
PubChem 1051
 1051
 		51
 51
 		44367445
 5960
 44367445
 5960
 		33032
 44272391
 88747398
 33032
 44272391
 88747398
 		970
 970
1aamA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1aawA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1aheA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1aheB01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1ahfA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1ahfB01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1ahgA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1ahgB01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1ahxA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1ahxB01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1ahyA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1ahyB01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1aiaA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1aiaB01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1aibA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1aibB01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1aicA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1aicB01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1ajrA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1ajrB01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1ajsA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1ajsB01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1akaA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1akaB01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1akbA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1akcA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1amaA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1amqA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1amrA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1amsA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1argA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1argB01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1arhA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1arhB01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1ariA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1ariB01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1arsA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1artA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1asaA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1asbA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1ascA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1asdA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1aseA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1asfA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1asgA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1aslA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1aslB01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1asmA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1asmB01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1asnA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1asnB01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1b4xA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1bjwA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1bjwB01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1bkgA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1bkgB01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1bkgC01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1bkgD01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1bqaA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1bqaB01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1bqdA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1bqdB01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1c9cA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1cq6A01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1cq7A01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1cq8A01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1czcA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1czeA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1g4vA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1g4xA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1g7wA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1g7xA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1ivrA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1mapA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1maqA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1oxoA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1oxoB01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1oxpA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1qirA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1qisA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1qitA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1spaA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1tarA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1tarB01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1tasA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1tasB01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1tatA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1tatB01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1yaaA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1yaaB01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1yaaC01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1yaaD01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1yooA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
2aatA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
2cstA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
2cstB01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
3aatA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
5eaaA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
7aatA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
7aatB01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
8aatA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
8aatB01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
9aatA01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
9aatB01 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1aamA02 Bound:PLP Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1aawA02 Bound:PLP Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1aheA02 Bound:PLP Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1aheB02 Bound:PLP Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1ahfA02 Bound:PLP Unbound Analogue:IOP Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1ahfB02 Bound:PLP Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1ahgA02 Bound:PLP Unbound Unbound Unbound Unbound Intermediate-analogue:PLP-TYR Unbound Unbound Unbound Unbound Unbound Unbound Intermediate-analogue:PLP-TYR
1ahgB02 Bound:PLP Unbound Unbound Unbound Unbound Intermediate-analogue:PLP-TYR Unbound Unbound Unbound Unbound Unbound Unbound Intermediate-analogue:PLP-TYR
1ahxA02 Bound:PLP Analogue:HCI Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1ahxB02 Bound:PLP Analogue:HCI Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1ahyA02 Bound:PLP Unbound Analogue:MAE Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1ahyB02 Bound:PLP Unbound Analogue:MAE Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1aiaA02 Analogue:PMP Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Intermediate-bound:PMP Unbound Unbound Unbound
1aiaB02 Analogue:PMP Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Intermediate-bound:PMP Unbound Unbound Unbound
1aibA02 Analogue:PMP Bound:AKG Unbound Unbound Unbound Unbound Unbound Unbound Unbound Intermediate-bound:PMP Unbound Unbound Unbound
1aibB02 Analogue:PMP Bound:AKG Unbound Unbound Unbound Unbound Unbound Unbound Unbound Intermediate-bound:PMP Unbound Unbound Unbound
1aicA02 Analogue:PMP Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Intermediate-bound:PMP Unbound Unbound Unbound
1aicB02 Analogue:PMP Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Intermediate-bound:PMP Unbound Unbound Unbound
1ajrA02 Bound:LLP Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1ajrB02 Bound:LLP Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1ajsA02 Analogue:PLA Unbound Unbound Unbound Unbound Intermediate-analogue:PLA Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1ajsB02 Bound:LLP Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1akaA02 Bound:PLP Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1akaB02 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1akbA02 Analogue:PPD Unbound Unbound Unbound Unbound Intermediate-Bound:PPD Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1akcA02 Analogue:PPE Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Intermediate-Bound:PPE
1amaA02 Analogue:PLA Unbound Unbound Unbound Unbound Intermediate-analogue:PLA Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1amqA02 Analogue:PMP Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Intermediate-bound:PMP Unbound Unbound Unbound
1amrA02 Analogue:PMP Unbound Analogue:MAE Unbound Unbound Unbound Unbound Unbound Unbound Intermediate-bound:PMP Unbound Unbound Unbound
1amsA02 Analogue:PMP Analogue:GUA Unbound Unbound Unbound Unbound Unbound Unbound Unbound Intermediate-bound:PMP Unbound Unbound Unbound
1argA02 Analogue:PPD Unbound Unbound Unbound Unbound Intermediate-Bound:PPD Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1argB02 Analogue:PPD Unbound Unbound Unbound Unbound Intermediate-Bound:PPD Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1arhA02 Analogue:PPD Unbound Unbound Unbound Unbound Intermediate-Bound:PPD Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1arhB02 Analogue:PPD Unbound Unbound Unbound Unbound Intermediate-Bound:PPD Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1ariA02 Bound:PLP Unbound Analogue:MAE Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1ariB02 Bound:PLP Unbound Analogue:MAE Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1arsA02 Bound:PLP Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1artA02 Bound:PLP Unbound Unbound Unbound Unbound Intermediate-analogue:PLP-ASP-CH3 Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1asaA02 Bound:PLP Unbound Analogue:MAE Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1asbA02 Bound:PLP Unbound Analogue:MAE Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1ascA02 Analogue:NPL Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Intermediate-analogue:NPL Unbound Unbound Unbound
1asdA02 Analogue:MPL Unbound Analogue:MAE Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1aseA02 Analogue:NOP Unbound Analogue:MAE Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1asfA02 Bound:PLP Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1asgA02 Bound:PLP Unbound Analogue:MAE Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1aslA02 Analogue:PLA Unbound Unbound Unbound Unbound Intermediate-analogue:PLA Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1aslB02 Analogue:PLA Unbound Unbound Unbound Unbound Intermediate-analogue:PLA Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1asmA02 Bound:PLP Unbound Analogue:MAE Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1asmB02 Bound:PLP Unbound Analogue:MAE Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1asnA02 Bound:PLP Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1asnB02 Bound:PLP Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1b4xA02 Bound:PLP Unbound Analogue:MAE Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1bjwA02 Bound:LLP Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1bjwB02 Bound:LLP Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1bkgA02 Analogue:PMP Unbound Analogue:MAE Unbound Unbound Unbound Unbound Unbound Unbound Intermediate-bound:PMP Unbound Unbound Unbound
1bkgB02 Analogue:PMP Unbound Analogue:MAE Unbound Unbound Unbound Unbound Unbound Unbound Intermediate-bound:PMP Unbound Unbound Unbound
1bkgC02 Analogue:PMP Unbound Analogue:MAE Unbound Unbound Unbound Unbound Unbound Unbound Intermediate-bound:PMP Unbound Unbound Unbound
1bkgD02 Analogue:PMP Unbound Analogue:MAE Unbound Unbound Unbound Unbound Unbound Unbound Intermediate-bound:PMP Unbound Unbound Unbound
1bqaA02 Bound:LLP Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1bqaB02 Bound:LLP Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1bqdA02 Bound:LLP Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1bqdB02 Bound:LLP Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1c9cA02 Analogue:PP3 Unbound Unbound Unbound Unbound Intermediate-analogue:PP3 Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1cq6A02 Analogue:PY4 Unbound Unbound Unbound Unbound Intermediate-analogue:PY4 Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1cq7A02 Analogue:PY5 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Intermediate-analogue:PY5
1cq8A02 Analogue:PY6 Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Intermediate-analogue:PY6
1czcA02 Bound:PLP Analogue:GUA Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1czeA02 Bound:PLP Unbound Analogue:SIN Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1g4vA02 Bound:PLP Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1g4xA02 Bound:PLP Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1g7wA02 Bound:PLP Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1g7xA02 Bound:PLP Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1ivrA02 Analogue:CBA Unbound Unbound Unbound Unbound Unbound Unbound Unbound Intermediate-analogue:CBA Unbound Unbound Unbound Unbound
1mapA02 Analogue:KET Unbound Unbound Unbound Unbound Unbound Unbound Intermediate-bound:KET Unbound Unbound Unbound Unbound Unbound
1maqA02 Analogue:PGU Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Intermediate-bound:PGU Unbound Unbound
1oxoA02 Analogue:IK2 Unbound Unbound Unbound Unbound Intermediate-analogue:IK2 Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1oxoB02 Analogue:IK2 Unbound Unbound Unbound Unbound Intermediate-analogue:IK2 Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1oxpA02 Analogue:IK2 Unbound Unbound Unbound Unbound Intermediate-analogue:IK2 Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1qirA02 Bound:PLP Unbound Analogue:MAE Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1qisA02 Bound:PLP Unbound Analogue:MAE Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1qitA02 Bound:PLP Unbound Analogue:MAE Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1spaA02 Analogue:NPL Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Intermediate-analogue:NPL Unbound Unbound Unbound
1tarA02 Bound:PLP Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1tarB02 Bound:PLP Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1tasA02 Analogue:PLA Unbound Unbound Unbound Unbound Intermediate-analogue:PLA Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1tasB02 Analogue:PLA Unbound Unbound Unbound Unbound Intermediate-analogue:PLA Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1tatA02 Bound:PLP Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1tatB02 Bound:PLP Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1yaaA02 Bound:PLP Unbound Analogue:MAE Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1yaaB02 Bound:PLP Unbound Analogue:MAE Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1yaaC02 Bound:PLP Unbound Analogue:MAE Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1yaaD02 Bound:PLP Unbound Analogue:MAE Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1yooA02 Bound:PLP Unbound Analogue:IVA Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
2aatA02 Analogue:PMP Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Intermediate-bound:PMP Unbound Unbound Unbound
2cstA02 Bound:PLP Unbound Analogue:MAE Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
2cstB02 Bound:PLP Unbound Analogue:MAE Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
3aatA02 Bound:PLP Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
5eaaA02 Bound:PLP Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
7aatA02 Bound:PLP Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
7aatB02 Bound:PLP Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
8aatA02 Bound:PLP Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
8aatB02 Bound:PLP Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound
9aatA02 Analogue:PMP Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Intermediate-bound:PMP Unbound Unbound Unbound
9aatB02 Analogue:PMP Unbound Unbound Unbound Unbound Unbound Unbound Unbound Unbound Intermediate-bound:PMP Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1aamA01
1aawA01
1aheA01 mutant V39L, K41Y, T47I
1aheB01 mutant V39L, K41Y, T47I
1ahfA01 mutant V39L, K41Y, T47I
1ahfB01 mutant V39L, K41Y, T47I
1ahgA01 mutant V39L, K41Y, T47I
1ahgB01 mutant V39L, K41Y, T47I
1ahxA01 mutant V39L, K41Y, T47I
1ahxB01 mutant V39L, K41Y, T47I
1ahyA01 mutant V39L, K41Y, T47I
1ahyB01 mutant V39L, K41Y, T47I
1aiaA01
1aiaB01
1aibA01
1aibB01
1aicA01
1aicB01
1ajrA01
1ajrB01
1ajsA01
1ajsB01
1akaA01
1akaB01
1akbA01
1akcA01
1amaA01
1amqA01
1amrA01
1amsA01
1argA01
1argB01
1arhA01
1arhB01
1ariA01
1ariB01
1arsA01
1artA01
1asaA01
1asbA01
1ascA01
1asdA01
1aseA01
1asfA01
1asgA01
1aslA01
1aslB01
1asmA01
1asmB01
1asnA01
1asnB01
1b4xA01
1bjwA01
1bjwB01
1bkgA01
1bkgB01
1bkgC01
1bkgD01
1bqaA01
1bqaB01
1bqdA01
1bqdB01
1c9cA01
1cq6A01
1cq7A01
1cq8A01
1czcA01
1czeA01
1g4vA01
1g4xA01
1g7wA01
1g7xA01
1ivrA01
1mapA01
1maqA01
1oxoA01
1oxoB01
1oxpA01
1qirA01
1qisA01
1qitA01
1spaA01
1tarA01
1tarB01
1tasA01
1tasB01
1tatA01
1tatB01
1yaaA01
1yaaB01
1yaaC01
1yaaD01
1yooA01 mutant A11T, F24L, N34D, I37M, K41N, I353T, S361F, S363G, V387L, M397L
2aatA01
2cstA01
2cstB01
3aatA01
5eaaA01
7aatA01
7aatB01
8aatA01
8aatB01
9aatA01
9aatB01
1aamA02 TYR 77;ASP 223;TYR 226;LYS 258 LYS 258(PLP binding) mutant R292D
1aawA02 TYR 77;ASP 223;TYR 226;LYS 258 LYS 258(PLP binding)
1aheA02 TYR 70;ASP 222;TYR 225;LYS 258 LYS 258(PLP binding) mutant N69L, T109S, N297S
1aheB02 TYR 70;ASP 222;TYR 225;LYS 258 LYS 258(PLP binding) mutant N69L, T109S, N297S
1ahfA02 TYR 70;ASP 222;TYR 225;LYS 258 LYS 258(PLP binding) mutant N69L, T109S, N297S
1ahfB02 TYR 70;ASP 222;TYR 225;LYS 258 LYS 258(PLP binding) mutant N69L, T109S, N297S
1ahgA02 TYR 70;ASP 222;TYR 225;LYS 258 LYS 258(PLP binding) mutant N69L, T109S, N297S
1ahgB02 TYR 70;ASP 222;TYR 225;LYS 258 LYS 258(PLP binding) mutant N69L, T109S, N297S
1ahxA02 TYR 70;ASP 222;TYR 225;LYS 258 LYS 258(PLP binding) mutant N69L, T109S, N297S
1ahxB02 TYR 70;ASP 222;TYR 225;LYS 258 LYS 258(PLP binding) mutant N69L, T109S, N297S
1ahyA02 TYR 70;ASP 222;TYR 225;LYS 258 LYS 258(PLP binding) mutant N69L, T109S, N297S
1ahyB02 TYR 70;ASP 222;TYR 225;LYS 258 LYS 258(PLP binding) mutant N69L, T109S, N297S
1aiaA02 TYR 70;ASP 222;TYR 225; mutant K258H
1aiaB02 TYR 70;ASP 222;TYR 225; mutant K258H
1aibA02 TYR 70;ASP 222;TYR 225; mutant K258H
1aibB02 TYR 70;ASP 222;TYR 225; mutant K258H
1aicA02 TYR 70;ASP 222;TYR 225; mutant K258H
1aicB02 TYR 70;ASP 222;TYR 225; mutant K258H
1ajrA02 TYR 70;ASP 222;TYR 225; LLP 258(PLP-binding Lys)
1ajrB02 TYR 70;ASP 222;TYR 225; LLP 258(PLP-binding Lys)
1ajsA02 TYR 70;ASP 222;TYR 225;LYS 258 LYS 258(PLP binding)
1ajsB02 TYR 70;ASP 222;TYR 225; LLP 258(PLP-binding Lys)
1akaA02 TYR 70;ASP 222;TYR 225; mutant K258H
1akaB02 TYR 70;ASP 222;TYR 225; mutant K258H
1akbA02 TYR 70;ASP 222;TYR 225; mutant K258H
1akcA02 TYR 70;ASP 222;TYR 225; mutant K258H
1amaA02 TYR 70;ASP 222;TYR 225;LYS 258 LYS 258(PLP binding)
1amqA02 TYR 70;ASP 222;TYR 225;LYS 258 LYS 258(PLP binding)
1amrA02 TYR 70;ASP 222;TYR 225;LYS 258 LYS 258(PLP binding)
1amsA02 TYR 70;ASP 222;TYR 225;LYS 258 LYS 258(PLP binding)
1argA02 TYR 70;ASP 222;TYR 225;LYS 258 LYS 258(PLP binding)
1argB02 TYR 70;ASP 222;TYR 225;LYS 258 LYS 258(PLP binding)
1arhA02 TYR 70;ASP 222;;LYS 258 LYS 258(PLP binding) mutant Y225R, R386A
1arhB02 TYR 70;ASP 222;;LYS 258 LYS 258(PLP binding) mutant Y225R, R386A
1ariA02 TYR 70;ASP 222;TYR 225;LYS 258 LYS 258(PLP binding) mutant W140H
1ariB02 TYR 70;ASP 222;TYR 225;LYS 258 LYS 258(PLP binding) mutant W140H
1arsA02 TYR 70;ASP 222;TYR 225;LYS 258 LYS 258(PLP binding)
1artA02 TYR 70;ASP 222;TYR 225;LYS 258 LYS 258(PLP binding)
1asaA02 TYR 77;ASP 223;TYR 226;LYS 258 LYS 258(PLP binding)
1asbA02 TYR 77; ;TYR 226;LYS 258 LYS 258(PLP binding) mutant D223A
1ascA02 TYR 77; ;TYR 226;LYS 258 LYS 258(PLP binding) mutant D223A
1asdA02 TYR 77;ASP 223;TYR 226;LYS 258 LYS 258(PLP binding)
1aseA02 TYR 77;ASP 223;TYR 226;LYS 258 LYS 258(PLP binding)
1asfA02 TYR 77;ASP 223;;LYS 258 LYS 258(PLP binding) mutant Y226F
1asgA02 TYR 77;ASP 223;;LYS 258 LYS 258(PLP binding) mutant Y226F
1aslA02 TYR 70;ASP 222;TYR 225;LYS 258 LYS 258(PLP binding)
1aslB02 TYR 70;ASP 222;TYR 225;LYS 258 LYS 258(PLP binding)
1asmA02 TYR 70;ASP 222;TYR 225;LYS 258 LYS 258(PLP binding)
1asmB02 TYR 70;ASP 222;TYR 225;LYS 258 LYS 258(PLP binding)
1asnA02 TYR 70;ASP 222;TYR 225;LYS 258 LYS 258(PLP binding)
1asnB02 TYR 70;ASP 222;TYR 225;LYS 258 LYS 258(PLP binding)
1b4xA02 TYR 70;ASP 222;TYR 225;LYS 258 LYS 258(PLP binding) mutant C191S
1bjwA02 TYR 64;ASP 203;TYR 206; LLP 234(PLP-binding Lys)
1bjwB02 TYR 64;ASP 203;TYR 206; LLP 234(PLP-binding Lys)
1bkgA02 TYR 64;ASP 203;TYR 206;LYS 234 LYS 234(PLP binding)
1bkgB02 TYR 64;ASP 203;TYR 206;LYS 234 LYS 234(PLP binding)
1bkgC02 TYR 64;ASP 203;TYR 206;LYS 234 LYS 234(PLP binding)
1bkgD02 TYR 64;ASP 203;TYR 206;LYS 234 LYS 234(PLP binding)
1bqaA02 TYR 70;ASP 222;TYR 225; LLP 258(PLP-binding Lys) mutant P195A
1bqaB02 TYR 70;ASP 222;TYR 225; LLP 258(PLP-binding Lys) mutant P195A
1bqdA02 TYR 70;ASP 222;TYR 225; LLP 258(PLP-binding Lys) mutant P138A, P195A
1bqdB02 TYR 70;ASP 222;TYR 225; LLP 258(PLP-binding Lys) mutant P138A, P195A
1c9cA02 TYR 70;ASP 222;TYR 225;LYS 258 LYS 258(PLP binding)
1cq6A02 TYR 70;ASP 222;TYR 225;LYS 258 LYS 258(PLP binding)
1cq7A02 TYR 70;ASP 222;TYR 225;LYS 258 LYS 258(PLP binding)
1cq8A02 TYR 70;ASP 222;TYR 225;LYS 258 LYS 258(PLP binding)
1czcA02 TYR 70;ASP 222;TYR 225;LYS 258 LYS 258(PLP binding)
1czeA02 TYR 70;ASP 222;TYR 225;LYS 258 LYS 258(PLP binding)
1g4vA02 TYR 70;ASP 222;;LYS 258 LYS 258(PLP binding) mutant N194A, Y225F
1g4xA02 TYR 70;ASP 222;TYR 225;LYS 258 LYS 258(PLP binding) mutant N194A, Y292L
1g7wA02 TYR 70;ASP 222;TYR 225;LYS 258 LYS 258(PLP binding) mutant N194A, R386L
1g7xA02 TYR 70;ASP 222;TYR 225;LYS 258 LYS 258(PLP binding) mutant N194A, R292L, R386L
1ivrA02 TYR 67;ASP 214;TYR 217;LYS 250 LYS 250(PLP binding)
1mapA02 TYR 70;ASP 222;TYR 225;LYS 258 LYS 258(PLP binding)
1maqA02 TYR 70;ASP 222;TYR 225;LYS 258 LYS 258(PLP binding)
1oxoA02 TYR 70;ASP 222;TYR 225;LYS 258 LYS 258(PLP binding)
1oxoB02 TYR 70;ASP 222;TYR 225;LYS 258 LYS 258(PLP binding)
1oxpA02 TYR 70;ASP 222;TYR 225;LYS 258 LYS 258(PLP binding)
1qirA02 TYR 70;ASP 222;TYR 225;LYS 258 LYS 258(PLP binding) mutant C191Y
1qisA02 TYR 70;ASP 222;TYR 225;LYS 258 LYS 258(PLP binding) mutant C191F
1qitA02 TYR 70;ASP 222;TYR 225;LYS 258 LYS 258(PLP binding) mutant C191W
1spaA02 TYR 70; ;TYR 225;LYS 258 LYS 258(PLP binding) mutant D222A
1tarA02 TYR 70;ASP 222;TYR 225;LYS 258 LYS 258(PLP binding)
1tarB02 TYR 70;ASP 222;TYR 225;LYS 258 LYS 258(PLP binding)
1tasA02 TYR 70;ASP 222;TYR 225;LYS 258 LYS 258(PLP binding)
1tasB02 TYR 70;ASP 222;TYR 225;LYS 258 LYS 258(PLP binding)
1tatA02 TYR 70;ASP 222;TYR 225;LYS 258 LYS 258(PLP binding)
1tatB02 TYR 70;ASP 222;TYR 225;LYS 258 LYS 258(PLP binding)
1yaaA02 TYR 70;ASP 222;TYR 225;LYS 258 LYS 258(PLP binding)
1yaaB02 TYR 70;ASP 222;TYR 225;LYS 258 LYS 258(PLP binding)
1yaaC02 TYR 70;ASP 222;TYR 225;LYS 258 LYS 258(PLP binding)
1yaaD02 TYR 70;ASP 222;TYR 225;LYS 258 LYS 258(PLP binding)
1yooA02 TYR 70;ASP 222;TYR 225;LYS 258 LYS 258(PLP binding) mutant K126R, S139G, N142T, A269T, A293V, N297S, S311G
2aatA02 TYR 77;ASP 223;TYR 226; mutant K258A
2cstA02 TYR 70;ASP 222;TYR 225;LYS 258 LYS 258(PLP binding)
2cstB02 TYR 70;ASP 222;TYR 225;LYS 258 LYS 258(PLP binding)
3aatA02 TYR 70;ASP 222;TYR 225;LYS 258 LYS 258(PLP binding) mutant R386F
5eaaA02 TYR 70;ASP 222;TYR 225;LYS 258 LYS 258(PLP binding) mutant C191S
7aatA02 TYR 70;ASP 222;TYR 225;LYS 258 LYS 258(PLP binding)
7aatB02 TYR 70;ASP 222;TYR 225;LYS 258 LYS 258(PLP binding)
8aatA02 TYR 70;ASP 222;TYR 225;LYS 258 LYS 258(PLP binding)
8aatB02 TYR 70;ASP 222;TYR 225;LYS 258 LYS 258(PLP binding)
9aatA02 TYR 70;ASP 222;TYR 225;LYS 258 LYS 258(PLP binding)
9aatB02 TYR 70;ASP 222;TYR 225;LYS 258 LYS 258(PLP binding)

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[3]
Scheme I, p.8648-8649
[5]
p.8163-8166
[7]
p.180-181
[9]
p.1984
[11]
[12]
Scheme 1
[13]
Scheme 2, p.574-576
[15]
Fig.1
[17]
Fig.1, p.5883-5886
[18]
Fig.1, p.510-514
[20]
Scheme 1, Scheme 2, p.115-116
[21]
Scheme I, p.13460-13461
[22]
Scheme 1, p.482-483
[24]
[26]
Scheme 2, p.1010-1011
[27]
Scheme 2, p.104-105
[30]
p.409-411
[32]
Scheme 1
[33]
Scheme 1, Chart 1, p.9419-9422
[34]
Scheme 1, p.413-414
[35]
Scheme 1, p.688-689
[39]
Fig.1, p.15265-15267
[46]
Scheme 1, p.15080-15085
[53]
Scheme 1
[59]
Scheme 1, Chart 1, p.356
[61]
Scheme I, Fig.5, p.9487-9488

References
[1]
Resource
Comments ACTIVE SITE
Medline ID 69285398
PubMed ID 5809231
Journal Biochemistry
Year 1969
Volume 8
Pages 3412-7
Authors Morino Y, Watanabe T
Title Primary structure of pyridoxal phosphate binding site in the mitochondrial and extramitochondrial aspartate aminotransferases from pig heart muscle. Chymotryptic peptides.
Related PDB
Related UniProtKB P00503
[2]
Resource
Comments ACTIVE SITE
Medline ID 73044407
PubMed ID 4634443
Journal FEBS Lett
Year 1972
Volume 23
Pages 262-4
Authors Polyanovsky OL, Demidkina TV
Title The position of an essential tyrosine residue in the polypeptide chain of aspartate transaminase.
Related PDB
Related UniProtKB P00503
[3]
Resource
Comments
Medline ID
PubMed ID 7410385
Journal J Biol Chem
Year 1980
Volume 255
Pages 8645-9
Authors Zito SW, Martinez-Carrion M
Title Stereospecificity of sodium borohydride reduction of Schiff bases at the active site of aspartate aminotransferase.
Related PDB
Related UniProtKB
[4]
Resource
Comments X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS)
Medline ID 80143195
PubMed ID 7360247
Journal Nature
Year 1980
Volume 284
Pages 189-90
Authors Borisov VV, Borisova SN, Sosfenov NI, Vainshtein BK
Title Electron density map of chicken heart cytosol aspartate transaminase at 3.5 A resolution.
Related PDB
Related UniProtKB P00504
[5]
Resource
Comments X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS)
Medline ID 82165126
PubMed ID 7067826
Journal FEBS Lett
Year 1982
Volume 138
Pages 113-6
Authors Harutyunyan EG, Malashkevich VN, Tersyan SS, Kochkina VM, Torchinsky YuM, Braunstein AE
Title Three-dimensional structure at 3.2 A resolution of the complex of cytosolic aspartate aminotransferase from chicken heart with 2-oxoglutarate.
Related PDB
Related UniProtKB P00504
[6]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF MUTANT ALA-246
Medline ID 90105323
PubMed ID 2513875
Journal Biochemistry
Year 1989
Volume 28
Pages 8161-7
Authors Smith DL, Almo SC, Toney MD, Ringe D
Title 2.8-A-resolution crystal structure of an active-site mutant of aspartate aminotransferase from Escherichia coli.
Related PDB 2aat
Related UniProtKB P00509
[7]
Resource
Comments
Medline ID
PubMed ID 2121725
Journal J Biochem (Tokyo)
Year 1990
Volume 108
Pages 175-84
Authors Kamitori S, Okamoto A, Hirotsu K, Higuchi T, Kuramitsu S, Kagamiyama H, Matsuura Y, Katsube Y
Title Three-dimensional structures of aspartate aminotransferase from Escherichia coli and its mutant enzyme at 2.5 A resolution.
Related PDB
Related UniProtKB
[8]
Resource
Comments
Medline ID
PubMed ID 2231709
Journal J Mol Biol
Year 1990
Volume 215
Pages 341-4
Authors Izard T, Fol B, Pauptit RA, Jansonius JN
Title Trigonal crystals of porcine mitochondrial aspartate aminotransferase.
Related PDB
Related UniProtKB
[9]
Resource
Comments X-RAY CRYSTALLOGRAPHY, AND MUTAGENESIS OF ARG-374
Medline ID 91129283
PubMed ID 1993208
Journal Biochemistry
Year 1991
Volume 30
Pages 1980-5
Authors Danishefsky AT, Onnufer JJ, Petsko GA, Ringe D
Title Activity and structure of the active-site mutants R386Y and R386F of Escherichia coli aspartate aminotransferase.
Related PDB 3aat
Related UniProtKB P00509
[10]
Resource
Comments
Medline ID
PubMed ID 2015218
Journal Biochemistry
Year 1991
Volume 30
Pages 3612-20
Authors Herold M, Leistler B, Hage A, Luger K, Kirschner K
Title Autonomous folding and coenzyme binding of the excised pyridoxal 5'-phosphate binding domain of aspartate aminotransferase from Escherichia coli.
Related PDB
Related UniProtKB
[11]
Resource
Comments MUTAGENESIS OF TYR-65
Medline ID 91329346
PubMed ID 1868057
Journal Biochemistry
Year 1991
Volume 30
Pages 7796-801
Authors Inoue K, Kuramitsu S, Okamoto A, Hirotsu K, Higuchi T, Kagamiyama H
Title Site-directed mutagenesis of Escherichia coli aspartate aminotransferase: role of Tyr70 in the catalytic processes.
Related PDB
Related UniProtKB P00509
[12]
Resource
Comments
Medline ID
PubMed ID 2007402
Journal Eur J Biochem
Year 1991
Volume 196
Pages 329-41
Authors Picot D, Sandmeier E, Thaller C, Vincent MG, Christen P, Jansonius JN
Title The open/closed conformational equilibrium of aspartate aminotransferase. Studies in the crystalline state and with a fluorescent probe in solution.
Related PDB
Related UniProtKB
[13]
Resource
Comments
Medline ID
PubMed ID 1869510
Journal J Biochem (Tokyo)
Year 1991
Volume 109
Pages 570-6
Authors Inoue K, Kuramitsu S, Okamoto A, Hirotsu K, Higuchi T, Morino Y, Kagamiyama H
Title Tyr225 in aspartate aminotransferase: contribution of the hydrogen bond between Tyr225 and coenzyme to the catalytic reaction.
Related PDB
Related UniProtKB
[14]
Resource
Comments
Medline ID
PubMed ID 1990006
Journal J Biol Chem
Year 1991
Volume 266
Pages 2567-72
Authors Sung MH, Tanizawa K, Tanaka H, Kuramitsu S, Kagamiyama H, Hirotsu K, Okamoto A, Higuchi T, Soda K
Title Thermostable aspartate aminotransferase from a thermophilic Bacillus species. Gene cloning, sequence determination, and preliminary x-ray characterization.
Related PDB
Related UniProtKB
[15]
Resource
Comments MUTAGENESIS OF HIS-133
Medline ID 91177849
PubMed ID 2007566
Journal J Biol Chem
Year 1991
Volume 266
Pages 6079-85
Authors Yano T, Kuramitsu S, Tanase S, Morino Y, Hiromi K, Kagamiyama H
Title The role of His143 in the catalytic mechanism of Escherichia coli aspartate aminotransferase.
Related PDB
Related UniProtKB P00509
[16]
Resource
Comments
Medline ID
PubMed ID 1920419
Journal J Mol Biol
Year 1991
Volume 221
Pages 61-3
Authors Malashkevich VN, Sinitzina NI
Title New crystal form of cytosolic chicken aspartate aminotransferase suitable for high-resolution X-ray analysis.
Related PDB
Related UniProtKB
[17]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 1610831
Journal Biochemistry
Year 1992
Volume 31
Pages 5878-87
Authors Yano T, Kuramitsu S, Tanase S, Morino Y, Kagamiyama H
Title Role of Asp222 in the catalytic mechanism of Escherichia coli aspartate aminotransferase: the amino acid residue which enhances the function of the enzyme-bound coenzyme pyridoxal 5'-phosphate.
Related PDB 1spa
Related UniProtKB
[18]
Resource
Comments X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS)
Medline ID 92277655
PubMed ID 1593633
Journal J Mol Biol
Year 1992
Volume 225
Pages 495-517
Authors McPhalen CA, Vincent MG, Jansonius JN
Title X-ray structure refinement and comparison of three forms of mitochondrial aspartate aminotransferase.
Related PDB 7aat 8aat 9aat
Related UniProtKB P00508
[19]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 1522585
Journal J Mol Biol
Year 1992
Volume 227
Pages 197-213
Authors McPhalen CA, Vincent MG, Picot D, Jansonius JN, Lesk AM, Chothia C
Title Domain closure in mitochondrial aspartate aminotransferase.
Related PDB 1ama
Related UniProtKB
[20]
Resource
Comments
Medline ID
PubMed ID 1339023
Journal Protein Sci
Year 1992
Volume 1
Pages 107-19
Authors Toney MD, Kirsch JF
Title Bronsted analysis of aspartate aminotransferase via exogenous catalysis of reactions of an inactive mutant.
Related PDB
Related UniProtKB
[21]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 7903048
Journal Biochemistry
Year 1993
Volume 32
Pages 13451-62
Authors Malashkevich VN, Toney MD, Jansonius JN
Title Crystal structures of true enzymatic reaction intermediates: aspartate and glutamate ketimines in aspartate aminotransferase.
Related PDB 1map 1maq
Related UniProtKB
[22]
Resource
Comments
Medline ID
PubMed ID 8436109
Journal Eur J Biochem
Year 1993
Volume 211
Pages 475-84
Authors Ziak M, Jager J, Malashkevich VN, Gehring H, Jaussi R, Jansonius JN, Christen P
Title Mutant aspartate aminotransferase (K258H) without pyridoxal-5'-phosphate-binding lysine residue. Structural and catalytic properties.
Related PDB
Related UniProtKB
[23]
Resource
Comments
Medline ID
PubMed ID 8227035
Journal J Biol Chem
Year 1993
Volume 268
Pages 24758-65
Authors Pan QW, Tanase S, Fukumoto Y, Nagashima F, Rhee S, Rogers PH, Arnone A, Morino Y
Title Functional roles of valine 37 and glycine 38 in the mobile loop of porcine cytosolic aspartate aminotransferase.
Related PDB
Related UniProtKB
[24]
Resource
Comments
Medline ID
PubMed ID 8263922
Journal J Mol Biol
Year 1993
Volume 234
Pages 1218-29
Authors Yano T, Hinoue Y, Chen VJ, Metzler DE, Miyahara I, Hirotsu K, Kagamiyama H
Title Role of an active site residue analyzed by combination of mutagenesis and coenzyme analog.
Related PDB
Related UniProtKB
[25]
Resource
Comments
Medline ID
PubMed ID 8112350
Journal Eur J Biochem
Year 1994
Volume 219
Pages 993-1000
Authors Sterk M, Hauser H, Marsh D, Gehring H
Title Probing conformational states of spin-labeled aspartate aminotransferase by ESR.
Related PDB
Related UniProtKB
[26]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 7896726
Journal J Biochem (Tokyo)
Year 1994
Volume 116
Pages 1001-12
Authors Miyahara I, Hirotsu K, Hayashi H, Kagamiyama H
Title X-ray crystallographic study of pyridoxamine 5'-phosphate-type aspartate aminotransferases from Escherichia coli in three forms.
Related PDB 1amq 1amr 1ams
Related UniProtKB
[27]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 7798192
Journal J Biochem (Tokyo)
Year 1994
Volume 116
Pages 95-107
Authors Okamoto A, Higuchi T, Hirotsu K, Kuramitsu S, Kagamiyama H
Title X-ray crystallographic study of pyridoxal 5'-phosphate-type aspartate aminotransferases from Escherichia coli in open and closed form.
Related PDB 1ars 1art
Related UniProtKB
[28]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 8120903
Journal J Mol Biol
Year 1994
Volume 236
Pages 963-8
Authors Hohenester E, Jansonius JN
Title Crystalline mitochondrial aspartate aminotransferase exists in only two conformations.
Related PDB 1tar 1tas 1tat
Related UniProtKB
[29]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 8196059
Journal J Mol Biol
Year 1994
Volume 239
Pages 285-305
Authors Jager J, Moser M, Sauder U, Jansonius JN
Title Crystal structures of Escherichia coli aspartate aminotransferase in two conformations. Comparison of an unliganded open and two liganded closed forms.
Related PDB 1asl 1asm 1asn
Related UniProtKB
[30]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 7909946
Journal Protein Eng
Year 1994
Volume 7
Pages 405-12
Authors Almo SC, Smith DL, Danishefsky AT, Ringe D
Title The structural basis for the altered substrate specificity of the R292D active site mutant of aspartate aminotransferase from E. coli.
Related PDB 1aam 1aaw 1asa 1asb 1asc 1asd 1ase 1asf
Related UniProtKB
[31]
Resource
Comments
Medline ID
PubMed ID 8073030
Journal Protein Eng
Year 1994
Volume 7
Pages 605-12
Authors Jager J, Pauptit RA, Sauder U, Jansonius JN
Title Three-dimensional structure of a mutant E. coli aspartate aminotransferase with increased enzymic activity.
Related PDB
Related UniProtKB
[32]
Resource
Comments
Medline ID
PubMed ID 7547975
Journal Biochemistry
Year 1995
Volume 34
Pages 12323-32
Authors Gloss LM, Kirsch JF
Title Examining the structural and chemical flexibility of the active site base, Lys-258, of Escherichia coli aspartate aminotransferase by replacement with unnatural amino acids.
Related PDB
Related UniProtKB
[33]
Resource
Comments
Medline ID
PubMed ID 7626611
Journal Biochemistry
Year 1995
Volume 34
Pages 9413-23
Authors Hayashi H, Kagamiyama H
Title Reaction of aspartate aminotransferase with L-erythro-3-hydroxyaspartate: involvement of Tyr70 in stabilization of the catalytic intermediates.
Related PDB
Related UniProtKB
[34]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 7819232
Journal Biochemistry
Year 1995
Volume 34
Pages 405-14
Authors Malashkevich VN, Jager J, Ziak M, Sauder U, Gehring H, Christen P, Jansonius JN
Title Structural basis for the catalytic activity of aspartate aminotransferase K258H lacking the pyridoxal 5'-phosphate-binding lysine residue.
Related PDB 1aia 1aib 1aic 1aka 1akb 1akc
Related UniProtKB
[35]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 7556224
Journal Eur J Biochem
Year 1995
Volume 232
Pages 686-90
Authors Graber R, Kasper P, Malashkevich VN, Sandmeier E, Berger P, Gehring H, Jansonius JN, Christen P
Title Changing the reaction specificity of a pyridoxal-5'-phosphate-dependent enzyme.
Related PDB 1arg 1arh
Related UniProtKB
[36]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 7851426
Journal Eur J Biochem
Year 1995
Volume 227
Pages 481-7
Authors Vacca RA, Christen P, Malashkevich VN, Jansonius JN, Sandmeier E
Title Substitution of apolar residues in the active site of aspartate aminotransferase by histidine. Effects on reaction and substrate specificity.
Related PDB 1ari
Related UniProtKB
[37]
Resource
Comments X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS)
Medline ID 95205406
PubMed ID 7897655
Journal J Mol Biol
Year 1995
Volume 247
Pages 111-24
Authors Malashkevich VN, Strokopytov BV, Borisov VV, Dauter Z, Wilson KS, Torchinsky YM
Title Crystal structure of the closed form of chicken cytosolic aspartate aminotransferase at 1.9 A resolution.
Related PDB 2cst
Related UniProtKB P00504
[38]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 7664122
Journal Nat Struct Biol
Year 1995
Volume 2
Pages 548-53
Authors Malashkevich VN, Onuffer JJ, Kirsch JF, Jansonius JN
Title Alternating arginine-modulated substrate specificity in an engineered tyrosine aminotransferase.
Related PDB 1ahe 1ahf 1ahg 1ahx 1ahy
Related UniProtKB
[39]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 8952476
Journal Biochemistry
Year 1996
Volume 35
Pages 15260-8
Authors von Stosch AG
Title Aspartate aminotransferase complexed with erythro-beta-hydroxyaspartate: crystallographic and spectroscopic identification of the carbinolamine intermediate.
Related PDB 1ivr
Related UniProtKB
[40]
Resource
Comments
Medline ID
PubMed ID 8856080
Journal Eur J Biochem
Year 1996
Volume 240
Pages 751-5
Authors Kasper P, Sterk M, Christen P, Gehring H
Title Molecular-dynamics simulation of domain movements in aspartate aminotransferase.
Related PDB
Related UniProtKB
[41]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 8665890
Journal Eur J Biochem
Year 1996
Volume 236
Pages 1025-32
Authors Markovic-Housley Z, Schirmer T, Hohenester E, Khomutov AR, Khomutov RM, Karpeisky MY, Sandmeier E, Christen P, Jansonius JN
Title Crystal structures and solution studies of oxime adducts of mitochondrial aspartate aminotransferase.
Related PDB 1oxo 1oxp
Related UniProtKB
[42]
Resource
Comments
Medline ID
PubMed ID 9012676
Journal Biochemistry
Year 1997
Volume 36
Pages 615-25
Authors Mollova ET, Metzler DE, Kintanar A, Kagamiyama H, Hayashi H, Hirotsu K, Miyahara I
Title Use of 1H-15N heteronuclear multiple-quantum coherence NMR spectroscopy to study the active site of aspartate aminotransferase.
Related PDB
Related UniProtKB
[43]
Resource
Comments X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS)
Medline ID 97362209
PubMed ID 9211866
Journal J Biol Chem
Year 1997
Volume 272
Pages 17293-302
Authors Rhee S, Silva MM, Hyde CC, Rogers PH, Metzler CM, Metzler DE, Arnone A
Title Refinement and comparisons of the crystal structures of pig cytosolic aspartate aminotransferase and its complex with 2-methylaspartate.
Related PDB 1ajr 1ajs
Related UniProtKB P00503
[44]
Resource
Comments
Medline ID
PubMed ID 9761867
Journal Acta Crystallogr D Biol Crystallogr
Year 1998
Volume 54
Pages 659-61
Authors Jeffery CJ, Barry T, Doonan S, Petsko GA, Ringe D
Title Crystallization and preliminary X-ray diffraction analysis of aspartate aminotransferase from Saccharomyces cerevisiae.
Related PDB
Related UniProtKB
[45]
Resource
Comments
Medline ID
PubMed ID 9757130
Journal Acta Crystallogr D Biol Crystallogr
Year 1998
Volume 54
Pages 1032-4
Authors Nakai T, Okada K, Kawaguchi S, Kato R, Kuramitsu S, Hirotsu K
Title Crystallization and preliminary X-ray characterization of aspartate aminotransferase from an extreme thermophile, Thermus thermophilus HB8.
Related PDB
Related UniProtKB
[46]
Resource
Comments
Medline ID
PubMed ID 9790670
Journal Biochemistry
Year 1998
Volume 37
Pages 15076-85
Authors Hayashi H, Mizuguchi H, Kagamiyama H
Title The imine-pyridine torsion of the pyridoxal 5'-phosphate Schiff base of aspartate aminotransferase lowers its pKa in the unliganded enzyme and is crucial for the successive increase in the pKa during catalysis.
Related PDB
Related UniProtKB
[47]
Resource
Comments
Medline ID
PubMed ID 9722549
Journal J Biol Chem
Year 1998
Volume 273
Pages 23191-202
Authors Mattingly JR Jr, Torella C, Iriarte A, Martinez-Carrion M
Title Conformation of aspartate aminotransferase isozymes folding under different conditions probed by limited proteolysis.
Related PDB
Related UniProtKB
[48]
Resource
Comments
Medline ID
PubMed ID 9792664
Journal J Biol Chem
Year 1998
Volume 273
Pages 29554-64
Authors Nobe Y, Kawaguchi S, Ura H, Nakai T, Hirotsu K, Kato R, Kuramitsu S
Title The novel substrate recognition mechanism utilized by aspartate aminotransferase of the extreme thermophile Thermus thermophilus HB8.
Related PDB
Related UniProtKB
[49]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS)
Medline ID 98318048
PubMed ID 9655342
Journal Protein Sci
Year 1998
Volume 7
Pages 1380-7
Authors Jeffery CJ, Barry T, Doonan S, Petsko GA, Ringe D
Title Crystal structure of Saccharomyces cerevisiae cytosolic aspartate aminotransferase.
Related PDB 1yaa
Related UniProtKB P23542
[50]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 9893985
Journal Biochemistry
Year 1999
Volume 38
Pages 905-13
Authors Birolo L, Malashkevich VN, Capitani G, De Luca F, Moretta A, Jansonius JN, Marino G
Title Functional and structural analysis of cis-proline mutants of Escherichia coli aspartate aminotransferase.
Related PDB 1bqa 1bqd
Related UniProtKB
[51]
Resource
Comments X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS)
Medline ID 99155214
PubMed ID 10029535
Journal Biochemistry
Year 1999
Volume 38
Pages 2413-24
Authors Nakai T, Okada K, Akutsu S, Miyahara I, Kawaguchi S, Kato R, Kuramitsu S, Hirotsu K
Title Structure of Thermus thermophilus HB8 aspartate aminotransferase and its complex with maleate.
Related PDB 1bjw 1bkg
Related UniProtKB Q56232
[52]
Resource
Comments
Medline ID
PubMed ID 10556573
Journal Biochim Biophys Acta
Year 1999
Volume 1434
Pages 191-201
Authors Mahon MM, Graber R, Christen P, Malthouse JP
Title The aspartate aminotransferase-catalysed exchange of the alpha-protons of aspartate and glutamate: the effects of the R386A and R292V mutations on this exchange reaction.
Related PDB
Related UniProtKB
[53]
Resource
Comments
Medline ID
PubMed ID 10531314
Journal J Biol Chem
Year 1999
Volume 274
Pages 31203-8
Authors Graber R, Kasper P, Malashkevich VN, Strop P, Gehring H, Jansonius JN, Christen P
Title Conversion of aspartate aminotransferase into an L-aspartate beta-decarboxylase by a triple active-site mutation.
Related PDB
Related UniProtKB
[54]
Resource
Comments
Medline ID
PubMed ID 9880502
Journal J Biol Chem
Year 1999
Volume 274
Pages 1320-5
Authors Mouratou B, Kasper P, Gehring H, Christen P
Title Conversion of tyrosine phenol-lyase to dicarboxylic amino acid beta-lyase, an enzyme not found in nature.
Related PDB
Related UniProtKB
[55]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF MUTANT
Medline ID 99107891
PubMed ID 9891001
Journal J Biol Chem
Year 1999
Volume 274
Pages 2344-9
Authors Oue S, Okamoto A, Yano T, Kagamiyama H
Title Redesigning the substrate specificity of an enzyme by cumulative effects of the mutations of non-active site residues.
Related PDB 1yoo
Related UniProtKB P00509
[56]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 10731702
Journal J Biochem (Tokyo)
Year 2000
Volume 127
Pages 337-43
Authors Oue S, Okamoto A, Yano T, Kagamiyama H
Title Cocrystallization of a mutant aspartate aminotransferase with a C5-dicarboxylic substrate analog: structural comparison with the enzyme-C4-dicarboxylic analog complex.
Related PDB 1czc 1cze
Related UniProtKB
[57]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 10858450
Journal J Biol Chem
Year 2000
Volume 275
Pages 18939-45
Authors Ishijima J, Nakai T, Kawaguchi S, Hirotsu K, Kuramitsu S
Title Free energy requirement for domain movement of an enzyme.
Related PDB 1c9c 1cq6 1cq7 1cq8
Related UniProtKB
[58]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 10708649
Journal Protein Eng
Year 2000
Volume 13
Pages 105-12
Authors Jeffery CJ, Gloss LM, Petsko GA, Ringe D
Title The role of residues outside the active site: structural basis for function of C191 mutants of Escherichia coli aspartate aminotransferase.
Related PDB 1b4x 1qir 1qis 1qit 5eaa
Related UniProtKB
[59]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 11148029
Journal Biochemistry
Year 2001
Volume 40
Pages 353-60
Authors Mizuguchi H, Hayashi H, Okada K, Miyahara I, Hirotsu K, Kagamiyama H
Title Strain is more important than electrostatic interaction in controlling the pKa of the catalytic group in aspartate aminotransferase.
Related PDB 1g4v 1g4x 1g7w 1g7x
Related UniProtKB
[60]
Resource
Comments
Medline ID
PubMed ID 11432784
Journal J Biochem (Tokyo)
Year 2001
Volume 130
Pages 89-98
Authors Ura H, Nakai T, Kawaguchi SI, Miyahara I, Hirotsu K, Kuramitsu S
Title Substrate recognition mechanism of thermophilic dual-substrate enzyme.
Related PDB
Related UniProtKB
[61]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 12488449
Journal J Biol Chem
Year 2003
Volume 278
Pages 9481-8
Authors Hayashi H, Mizuguchi H, Miyahara I, Nakajima Y, Hirotsu K, Kagamiyama H
Title Conformational change in aspartate aminotransferase on substrate binding induces strain in the catalytic group and enhances catalysis.
Related PDB 1ix6 1ix7 1ix8
Related UniProtKB

Comments
This enzyme belongs to the Aspartate aminotransferase (AAT) subclass of type-I PLP-dependent enzyme superfamily (Aspartate aminotransferase superfamily; AAT).
This enzyme catalyzes transamination, which is composed of the following reactions:
(A) Formation of external aldimine (with amine group of L-Aspartate),
(B) Isomerization (change in the position of double-bond), forming a ketimine intermediate.
(C) Schiff-base deforming by hydration, releasing the first product, oxaloacetate, and PMP.
(D) Schiff-base forming of PMP with carbonyl group of the second substrate, 2-oxoglutarate, leading again to a ketimine intermediate.
(E) Isomerization (change in the position of double-bond).
(F) Formation of internal aldimine, leading to the elimination of the product from PLP.
These reactions proceed in the following way:
(A) Formation of external aldimine (with amine group of L-Aspartate) (see [11], [13], [18] & [46])
(A1) Tyr225 interacts with O3' atom of PLP, when the PLP-aldimine is protonated, modulating and keeping the O3' of PLP negatively charged (see [13]).
(A2) The negatively charged O3 atom of PLP modulates the pKa of the alpha-amino group of substrate, L-aspartate, and also the pKa of the internal aldimine with Lys258. Here, according to the literature [46], [59] & [61], the imine-pyridine torsion (or strain) of PLP-Schiff base lowers pKa of the internal aldimine, without lowering the external aldimine. In any case, the difference in the pKa values facilitates the proton transfer from the alpha-amino group of L-aspartate to the NZ nitrogen of Lys258.
(A3) The deprotonated amine group of L-aspartate makes a nucleophilic attack on the C4' carbon of PLP, forming a transient geminal diamine intermediate.
(A4) There must be a general base, which deprotonates the amine group of the previously L-aspartate substrate, so that the lone pair of the amine group can attack on the C4' atom to form a double-bond, and to release the amine of the catalytic residue, Lys258. Considering the active-site structure, Tyr70' (from the adjacent chain) may play the role as the general base, although the literature has not mentioned it (except for the literature [11]). (The released Lys258 must be deprotonated, so that it can act as a general base at the next stage.)
(A5) The reaction produces the external aldimine with L-aspartate.
(B) Isomerization (change in the position of double-bond), forming a ketimine intermediate (see [17], [18], [20], [21], [22] & [24]).
(B1) Asp222 interacts with the N1 atom of PLP, modulating and enhancing the activity of the PLP cofactor as an electron sink, which facilitates the abstraction of alpha-proton from the aspartate covalently bound to the PLP (see [17] & [24]). At the same time, Tyr225 also interacts with the O3' atom of the PLP, modulating the activity of the PLP (see [13]).
(B2) Lys258 acts as a general base to deprotonate the alpha-proton of the amino acid substrate, forming a quinonoid intermediate.
(B3) Lys258 acts as a general acid to protonate the C4' atom of the PLP, leading to the formation of a ketimine intermediate.
(C) Schiff-base deforming by hydration, releasing the first product, oxaloacetate, and PMP (see [18] & [26]).
(C1) Lys258 acts as a general base to activate a water (at the si-face side of cofactor).
(C2) The activated water molecule makes a nucleophilic attack on the alpha-carbon atom of the substrate (from the si-face side), forming a carbinolamine intermediate.
(C3) Lys258 may act as a general acid to protonate the N4' atom of the PLP. Tyr225 may modulate the activity of Lys258. (Tyr225 is hydrogen-bonded to the O3 atom of the PLP).
(C4) The lone pair of the hydroxyl oxygen makes a nucleophilic attack on the C4' atom, whereas Lys258 acts as a general base to deprotonate the hydroxyl group, releasing the first product, oxaloacetate and the PMP.
(D) Schiff-base forming of PMP with carbonyl group of the second substrate (see [18] & [26])
(D1) The second substrate, 2-oxoglutarate, is bound to the active site, with the carbonyl oxygen hydrogen-bonded by Lys258.
(D2) The amine group (or the N4' atom) of PMP is unprotonated and makes a nucleophilic attack on the carbonyl carbon of the substrate, whereas Lys258 acts as a general acid to protonate the carbonyl oxygen, forming a carbinolamine intermediate.
(D3) Lys258 acts as a general base to deprotonate the N4 amine group. Tyr225 may modulate the activity of Lys258. (Tyr225 is hydrogen-bonded to the O3 atom of the PLP).
(D4) The lone pair of the N4' nitrogen atom makes a nucleophilic attack on the carbon atom, whereas Lys258 acts as a general acid to the hydroxyl group of the carbinolamine intermediate, leading to the cleavage between the carbon and the N4' atom, and to the release of a water moleucle. This reaction gives a ketimine intermediate again.
(E) Isomerization (change in the position of double-bond): (Inverse reaction of (B))
(E1) Asp222 modulates and enhances the activity of the PLP cofactor as an electron sink, which facilitates the abstraction of alpha-proton from the C4' atom of the PLP.
(E2) Lys258 acts as a general base to deprotonate the C4' atom of the PLP, leading to the formation of a quinonoid intermediate.
(E3) Lys258 acts as a general acid to protonate the alpha-proton of the amino acid substrate, forming an external aldimine. (As a result, Lys258 must be deprotonated, so that it can act as a general base at the next stage.)
(F) Formation of internal aldimine, leading to the elimination of the product from PLP: (Inverse reaction of (A))
(F1) Tyr225 interacts with O3' atom of PLP, when the PLP-aldimine is protonated, modulating and keeping the O3' of PLP negatively charged (see [13]).
(F2) The deprotonated amine group of Lys258 makes a nucleophilic attack on the C4' carbon of the PLP of the external aldimine, forming a transient geminal diamine intermediate. On the other hand, there must be a general acid, which protonates the N4' nitrogen atom of the external aldimine or the geminal diamine. Considering the active-site structure, Tyr70' (from the adjacent chain) may play the role as the general acid, although the literature has not mentioned it (except for the literature [11]).
(F3) The lone pair of the amine nitrogen of Lys258 can attack on the C4' atom to form a double-bond, and to release the amine of the second product, L-glutamate.
(F4) The negatively charged O3 atom of PLP modulates the pKa of the alpha-amino group of product, L-glutamate, and also the pKa of the internal aldimine with Lys258. In any case, the difference in the pKa values facilitates the proton transfer from the NZ nitrogen of Lys258 to the alpha-amine group of L-glutarate.
The pKas of the related groups are as follows (see [46]):
Unliganded internal aldimine; 6.8
Internal aldimine complexed with substrate/product; 8.1
External aldimine; 10.2

Created Updated
2004-10-21 2009-02-26