DB code: D00269

CATH domain 3.90.1150.10 : Aspartate Aminotransferase, domain 1
3.40.640.10 : Aspartate Aminotransferase; domain 2 Catalytic domain
E.C. 4.4.1.14
CSA 1b8g
M-CSA 1b8g
MACiE

CATH domain Related DB codes (homologues)
3.40.640.10 : Aspartate Aminotransferase; domain 2 D00085 D00092 D00101 D00102 D00103 D00104 D00107 D00108 D00109 D00255 D00257 D00258 D00265 D00515 M00031 D00279
3.90.1150.10 : Aspartate Aminotransferase, domain 1 D00085 D00092 D00101 D00102 D00103 D00104 D00107 D00108 D00109 D00255 D00257 D00258 D00265 D00515 M00031 D00279

Uniprot Enzyme Name
UniprotKB Protein name Synonyms Pfam
P37821 1-aminocyclopropane-1-carboxylate synthase
ACC synthase
EC 4.4.1.14
S-adenosyl-L-methionine methylthioadenosine-lyase
PF00155 (Aminotran_1_2)
[Graphical View]
P18485 1-aminocyclopropane-1-carboxylate synthase 2
ACC synthase 2
EC 4.4.1.14
Le-ACS2
ACS-2
S-adenosyl-L-methionine methylthioadenosine-lyase 2
PF00155 (Aminotran_1_2)
[Graphical View]

KEGG enzyme name
1-aminocyclopropane-1-carboxylate synthase
1-aminocyclopropanecarboxylate synthase
1-aminocyclopropane-1-carboxylic acid synthase
1-aminocyclopropane-1-carboxylate synthetase
aminocyclopropanecarboxylic acid synthase
aminocyclopropanecarboxylate synthase
ACC synthase
S-adenosyl-L-methionine methylthioadenosine-lyase

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P37821 1A1C_MALDO S-adenosyl-L-methionine = 1-aminocyclopropane- 1-carboxylate + methylthioadenosine. Homodimer. Pyridoxal phosphate.
P18485 1A12_SOLLC S-adenosyl-L-methionine = 1-aminocyclopropane- 1-carboxylate + methylthioadenosine. Homodimer and heterodimer. In vivo, the relevance of heterodimerization with other ACS enzymes is however unsure. Pyridoxal phosphate.

KEGG Pathways
Map code Pathways E.C.
MAP00271 Methionine metabolism

Compound table
Cofactors Substrates Products Intermediates
KEGG-id C00018 C00019 C01234 C00170
E.C.
Compound Pyridoxal phosphate S-Adenosyl-L-methionine 1-Aminocyclopropane-1-carboxylate Methylthioadenosine
Type aromatic ring (with nitrogen atoms),phosphate group/phosphate ion amino acids,amine group,nucleoside,sulfonium ion amino acids amine group,nucleoside,sulfide group
ChEBI 18405
 18405
 		67040
 67040
 		18053
 58360
 18053
 58360
 		17509
 17509
PubChem 1051
 1051
 		34755
 34755
 		535
 6971063
 535
 6971063
 		439176
 439176
1b8gA01 Unbound Unbound Unbound Unbound Unbound
1b8gB01 Unbound Unbound Unbound Unbound Unbound
1m7yA01 Unbound Unbound Unbound Unbound Unbound
1m4nA01 Unbound Unbound Unbound Unbound Unbound
1iaxA01 Unbound Unbound Unbound Unbound Unbound
1iaxB01 Unbound Unbound Unbound Unbound Unbound
1iayA01 Unbound Unbound Unbound Unbound Unbound
1b8gA02 Bound:PLP Unbound Unbound Unbound Unbound
1b8gB02 Bound:PLP Unbound Unbound Unbound Unbound
1m7yA02 Analogue:PPG Unbound Unbound Unbound Intermediate-analogue:PPG
1m4nA02 Bound:PLP Analogue:AAD Unbound Unbound Intermediate-analogue:PLP-AAD
1iaxA02 Bound:PLP Unbound Unbound Unbound Unbound
1iaxB02 Bound:PLP Unbound Unbound Unbound Unbound
1iayA02 Bound:PLP Unbound Analogue:AVG Unbound Unbound

Reference for Active-site residues
resource references E.C.
literature [9] & [11]

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1b8gA01
1b8gB01
1m7yA01
1m4nA01
1iaxA01
1iaxB01
1iayA01
1b8gA02 TYR 145;LYS 273 LYS 273(PLP binding)
1b8gB02 TYR 145;LYS 273 LYS 273(PLP binding)
1m7yA02 TYR 145;LYS 273 LYS 273(PLP binding)
1m4nA02 TYR 145;LYS 273 LYS 273(PLP binding)
1iaxA02 TYR 152;LYS 278 LYS 278(PLP binding)
1iaxB02 TYR 152;LYS 278 LYS 278(PLP binding)
1iayA02 TYR 152;LYS 278 LYS 278(PLP binding)

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[1]
Fig.4, p.7824
[7]
Scheme 4B, Scheme 6, p.15486-15487
[8]
p.8
[9]
Scheme 2, p.748-749 4
[10]
Scheme 1, Scheme 3A, p.12283 3
[11]
p.38214, Fig.6, p.38215 5
[12]
Scheme 3, p.3840-3841

References
[1]
Resource
Comments
Medline ID
PubMed ID 3865199
Journal Proc Natl Acad Sci U S A
Year 1985
Volume 82
Pages 7820-4
Authors Ramalingam K, Lee KM, Woodard RW, Bleecker AB, Kende H
Title Stereochemical course of the reaction catalyzed by the pyridoxal phosphate-dependent enzyme 1-aminocyclopropane-1-carboxylate synthase.
Related PDB
Related UniProtKB
[2]
Resource
Comments
Medline ID
PubMed ID 2712568
Journal Arch Biochem Biophys
Year 1989
Volume 271
Pages 107-12
Authors Satoh S, Yang SF
Title Specificity of S-adenosyl-L-methionine in the inactivation and the labeling of 1-aminocyclopropane-1-carboxylate synthase isolated from tomato fruits.
Related PDB
Related UniProtKB
[3]
Resource
Comments
Medline ID
PubMed ID 1421146
Journal Plant Mol Biol
Year 1992
Volume 20
Pages 425-36
Authors Botella JR, Arteca JM, Schlagnhaufer CD, Arteca RN, Phillips AT
Title Identification and characterization of a full-length cDNA encoding for an auxin-induced 1-aminocyclopropane-1-carboxylate synthase from etiolated mung bean hypocotyl segments and expression of its mRNA in response to indole-3-acetic acid.
Related PDB
Related UniProtKB
[4]
Resource
Comments
Medline ID
PubMed ID 7966311
Journal J Mol Biol
Year 1994
Volume 243
Pages 947-9
Authors Hohenester E, White MF, Kirsch JF, Jansonius JN
Title Crystallization and preliminary X-ray analysis of recombinant 1-aminocyclopropane-1-carboxylate synthase from apple. A key enzyme in the biosynthesis of the plant hormone ethylene.
Related PDB
Related UniProtKB
[5]
Resource
Comments
Medline ID
PubMed ID 7809054
Journal Proc Natl Acad Sci U S A
Year 1994
Volume 91
Pages 12428-32
Authors White MF, Vasquez J, Yang SF, Kirsch JF
Title Expression of apple 1-aminocyclopropane-1-carboxylate synthase in Escherichia coli: kinetic characterization of wild-type and active-site mutant forms.
Related PDB
Related UniProtKB
[6]
Resource
Comments
Medline ID
PubMed ID 8557119
Journal FEBS Lett
Year 1996
Volume 378
Pages 286-90
Authors Li N, Huxtable S, Yang SF, Kung SD
Title Effects of N-terminal deletions on 1-aminocyclopropane-1-carboxylate synthase activity.
Related PDB
Related UniProtKB
[7]
Resource
Comments
Medline ID
PubMed ID 9398277
Journal Biochemistry
Year 1997
Volume 36
Pages 15477-88
Authors Li Y, Feng L, Kirsch JF
Title Kinetic and spectroscopic investigations of wild-type and mutant forms of apple 1-aminocyclopropane-1-carboxylate synthase.
Related PDB
Related UniProtKB
[8]
Resource
Comments
Medline ID
PubMed ID 9279127
Journal Indian J Exp Biol
Year 1997
Volume 35
Pages 1-17
Authors Penrose DM, Glick BR
Title Enzymes that regulate ethylene levels--1-aminocyclopropane-1-carboxylic acid (ACC) deaminase, ACC synthase and ACC oxidase.
Related PDB
Related UniProtKB
[9]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.37 ANGSTROMS)
Medline ID 20079531
PubMed ID 10610793
Journal J Mol Biol
Year 1999
Volume 294
Pages 745-56
Authors Capitani G, Hohenester E, Feng L, Storici P, Kirsch JF, Jansonius JN
Title Structure of 1-aminocyclopropane-1-carboxylate synthase, a key enzyme in the biosynthesis of the plant hormone ethylene.
Related PDB 1b8g
Related UniProtKB P37821
[10]
Resource
Comments
Medline ID
PubMed ID 11591146
Journal Biochemistry
Year 2001
Volume 40
Pages 12276-84
Authors McCarthy DL, Capitani G, Feng L, Gruetter MG, Kirsch JF
Title Glutamate 47 in 1-aminocyclopropane-1-carboxylate synthase is a major specificity determinant.
Related PDB
Related UniProtKB
[11]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 11431475
Journal J Biol Chem
Year 2001
Volume 276
Pages 38210-6
Authors Huai Q, Xia Y, Chen Y, Callahan B, Li N, Ke H
Title Crystal structures of 1-aminocyclopropane-1-carboxylate (ACC) synthase in complex with aminoethoxyvinylglycine and pyridoxal-5'-phosphate provide new insight into catalytic mechanisms.
Related PDB 1iax
Related UniProtKB
[12]
Resource
Comments
Medline ID
PubMed ID 11888303
Journal Biochemistry
Year 2002
Volume 41
Pages 3836-42
Authors Eliot AC, Kirsch JF
Title Modulation of the internal aldimine pK(a)'s of 1-aminocyclopropane-1-carboxylate synthase and aspartate aminotransferase by specific active site residues.
Related PDB
Related UniProtKB
[13]
Resource
Comments
Medline ID
PubMed ID 12228256
Journal J Biol Chem
Year 2002
Volume 277
Pages 49735-42
Authors Capitani G, McCarthy DL, Gut H, Grutter MG, Kirsch JF
Title Apple 1-aminocyclopropane-1-carboxylate synthase in complex with the inhibitor L-aminoethoxyvinylglycine. Evidence for a ketimine intermediate.
Related PDB 1m7y
Related UniProtKB
[14]
Resource
Comments
Medline ID
PubMed ID 12686108
Journal Biochim Biophys Acta
Year 2003
Volume 1647
Pages 55-60
Authors Capitani G, Eliot AC, Gut H, Khomutov RM, Kirsch JF, Grutter MG
Title Structure of 1-aminocyclopropane-1-carboxylate synthase in complex with an amino-oxy analogue of the substrate: implications for substrate binding.
Related PDB 1m4n
Related UniProtKB

Comments
This enzyme catalyzes a PLP-dependent elimination reaction, followed by an isomerization reaction.

Created Updated
2004-05-24 2009-02-26