DB code: D00106
| RLCP classification | 6.30.115020.5300 : Double-bonded atom exchange | |
|---|---|---|
| 6.20.93000.5520 : Double-bonded atom exchange | ||
| CATH domain | 3.30.470.10 : D-amino Acid Aminotransferase; Chain A, domain 1 | |
| 3.20.10.10 : D-amino Acid Aminotransferase; Chain A, domain 2 | Catalytic domain | |
| E.C. | 2.6.1.42 | |
| CSA | 1iyd | |
| M-CSA | 1iyd | |
| MACiE | ||
| CATH domain | Related DB codes (homologues) |
|---|---|
| 3.20.10.10 : D-amino Acid Aminotransferase; Chain A, domain 2 | D00105 |
| 3.30.470.10 : D-amino Acid Aminotransferase; Chain A, domain 1 | D00105 |
| Uniprot Enzyme Name | UniprotKB | Protein name | Synonyms | RefSeq | Pfam |
|---|---|---|---|---|
| P0AB80 |
Branched-chain-amino-acid aminotransferase
|
BCAT
EC 2.6.1.42 Transaminase B |
YP_026247.1
(Protein)
NC_000913.2 (DNA/RNA sequence) YP_491668.1 (Protein) NC_007779.1 (DNA/RNA sequence) |
PF01063
(Aminotran_4)
[Graphical View] |
| O15382 |
Branched-chain-amino-acid aminotransferase, mitochondrial
|
BCAT(m)
EC 2.6.1.42 Placental protein 18 PP18 |
NP_001158245.1
(Protein)
NM_001164773.1 (DNA/RNA sequence) NP_001181.2 (Protein) NM_001190.3 (DNA/RNA sequence) |
PF01063
(Aminotran_4)
[Graphical View] |
| KEGG enzyme name |
|---|
|
branched-chain-amino-acid transaminase
transaminase B branched-chain amino acid aminotransferase branched-chain amino acid-glutamate transaminase branched-chain aminotransferase L-branched chain amino acid aminotransferase glutamate-branched-chain amino acid transaminase |
| UniprotKB: Accession Number | Entry name | Activity | Subunit | Subcellular location | Cofactor |
|---|---|---|---|---|---|
| P0AB80 | ILVE_ECOLI | L-leucine + 2-oxoglutarate = 4-methyl-2- oxopentanoate + L-glutamate. 2-oxoglutaric acid + L-isoleucine = (S)-3- methyl-2-oxopentanoic acid + L-glutamic acid. 2-oxoglutaric acid + L-valine = 3-methyl-2- oxobutanoic acid + L-glutamic acid. | Homohexamer. | Pyridoxal phosphate. | |
| O15382 | BCAT2_HUMAN | L-leucine + 2-oxoglutarate = 4-methyl-2- oxopentanoate + L-glutamate. 2-oxoglutaric acid + L-isoleucine = (S)-3- methyl-2-oxopentanoic acid + L-glutamic acid. 2-oxoglutaric acid + L-valine = 3-methyl-2- oxobutanoic acid + L-glutamic acid. | Homodimer. | Isoform A: Mitochondrion. Isoform B: Cytoplasm. | Pyridoxal phosphate. |
| KEGG Pathways | Map code | Pathways | E.C. |
|---|---|---|
| MAP00280 | Valine, leucine and isoleucine degradation | |
| MAP00290 | Valine, leucine and isoleucine biosynthesis | |
| MAP00770 | Pantothenate and CoA biosynthesis |
| Compound table | ||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Cofactors | Substrates | Products | Intermediates | |||||||||||||||
| KEGG-id | C00018 | C00123 | C00407 | C00183 | C00026 | C00233 | C03465 | C00141 | C00025 | |||||||||
| E.C. | ||||||||||||||||||
| Compound | Pyridoxal phosphate | L-Leucine | L-Isoleucine | L-Valine | 2-Oxoglutarate | 4-Methyl-2-oxopentanoate | 3-Methyl-2-oxopentanoate | 3-Methyl-2-oxobutanoate | L-Glutamate | External aldimine | Quinonoid intermediate | Ketimine intermediate | Carbinolamine intermediate | |||||
| Type | aromatic ring (with nitrogen atoms),phosphate group/phosphate ion | amino acids | amino acids | amino acids | carbohydrate,carboxyl group | carbohydrate,carboxyl group | carbohydrate,carboxyl group | carbohydrate,carboxyl group | amino acids,carboxyl group | |||||||||
| ChEBI |
18405 18405 |
15603 57427 15603 57427 |
17191 58045 17191 58045 |
16414 57762 16414 57762 |
30915 30915 |
48430 48430 |
35932 35932 |
16530 16530 |
16015 16015 |
|||||||||
| PubChem |
1051 1051 |
6106 7045798 6106 7045798 |
6306 7043901 6306 7043901 |
6287 6971018 88733505 6287 6971018 88733505 |
51 51 |
70 70 |
47 47 |
49 49 |
33032 44272391 88747398 33032 44272391 88747398 |
|||||||||
| 1a3gA01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1a3gB01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1a3gC01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1i1kA01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1i1kB01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1i1kC01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1i1lA01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1i1lB01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1i1lC01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1i1mA01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1i1mB01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1i1mC01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1iydA01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Analogue:GUA | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1iydB01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Analogue:GUA | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1iydC01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Analogue:GUA | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1iyeA01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1iyeB01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1iyeC01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1ekfA01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1ekfB01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1ekpA01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1ekpB01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1ekvA01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1ekvB01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1kt8A01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1kt8B01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1ktaA01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1ktaB01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1a3gA02 |
|
|
|
|
|
Bound:PLP | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1a3gB02 |
|
|
|
|
|
Bound:PLP | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1a3gC02 |
|
|
|
|
|
Bound:PLP | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1i1kA02 |
|
|
|
|
|
Bound:PLP | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1i1kB02 |
|
|
|
|
|
Bound:PLP | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1i1kC02 |
|
|
|
|
|
Bound:PLP | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1i1lA02 |
|
|
|
|
|
Bound:PLP | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Intermediate-analogue:PLP-2ML | Unbound | Unbound | Unbound |
| 1i1lB02 |
|
|
|
|
|
Bound:PLP | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Intermediate-analogue:PLP-2ML | Unbound | Unbound | Unbound |
| 1i1lC02 |
|
|
|
|
|
Bound:PLP | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Intermediate-analogue:PLP-2ML | Unbound | Unbound | Unbound |
| 1i1mA02 |
|
|
|
|
|
Bound:PLP | Unbound | Unbound | Analogue:4MV | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1i1mB02 |
|
|
|
|
|
Bound:PLP | Unbound | Unbound | Analogue:4MV | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1i1mC02 |
|
|
|
|
|
Bound:PLP | Unbound | Unbound | Analogue:4MV | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1iydA02 |
|
|
|
|
|
Bound:PLP | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1iydB02 |
|
|
|
|
|
Bound:PLP | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1iydC02 |
|
|
|
|
|
Bound:PLP | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1iyeA02 |
|
|
|
|
|
Analogue:PGU | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Intermediate-analogue:PGU | Unbound | Unbound |
| 1iyeB02 |
|
|
|
|
|
Analogue:PGU | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Intermediate-analogue:PGU | Unbound | Unbound |
| 1iyeC02 |
|
|
|
|
|
Analogue:PGU | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Intermediate-analogue:PGU | Unbound | Unbound |
| 1ekfA02 |
|
|
|
|
|
Bound:PLP | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1ekfB02 |
|
|
|
|
|
Bound:PLP | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1ekpA02 |
|
|
|
|
|
Bound:PLP | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1ekpB02 |
|
|
|
|
|
Bound:PLP | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1ekvA02 |
|
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|
|
|
Bound:PLP | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Intermediate-analogue:PLP-TRS |
| 1ekvB02 |
|
|
|
|
|
Bound:PLP | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Intermediate-analogue:PLP-TRS |
| 1kt8A02 |
|
|
|
|
|
Analogue:ILP | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Intermediate-bound:ILP | Unbound |
| 1kt8B02 |
|
|
|
|
|
Analogue:ILP | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Intermediate-bound:ILP | Unbound |
| 1ktaA02 |
|
|
|
|
|
Analogue:PMP | Unbound | Unbound | Unbound | Analogue:KIV | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| 1ktaB02 |
|
|
|
|
|
Analogue:PMP | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound | Unbound |
| Reference for Active-site residues | ||
|---|---|---|
| resource | references | E.C. |
| Swiss-prot | ||
| Active-site residues | ||||||||||
|---|---|---|---|---|---|---|---|---|---|---|
| PDB | Catalytic residues | Cofactor-binding residues | Modified residues | Main-chain involved in catalysis | Comment | |||||
| 1a3gA01 |
|
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| 1a3gB01 |
|
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| 1a3gC01 |
|
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| 1i1kA01 |
|
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| 1i1kB01 |
|
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| 1i1kC01 |
|
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| 1i1lA01 |
|
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| 1i1lB01 |
|
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| 1i1lC01 |
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| 1i1mA01 |
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| 1i1mB01 |
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| 1i1mC01 |
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| 1iydA01 |
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| 1iydB01 |
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| 1iydC01 |
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| 1iyeA01 |
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| 1iyeB01 |
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| 1iyeC01 |
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| 1ekfA01 |
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| 1ekfB01 |
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| 1ekpA01 |
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| 1ekpB01 |
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| 1ekvA01 |
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| 1ekvB01 |
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| 1kt8A01 |
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| 1kt8B01 |
|
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| 1ktaA01 |
|
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| 1ktaB01 |
|
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| 1a3gA02 |
|
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|
LYS 159;TYR 164 | LYS 159(PLP binding) | |||
| 1a3gB02 |
|
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|
LYS 159;TYR 164 | LYS 159(PLP binding) | |||
| 1a3gC02 |
|
|
|
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|
LYS 159;TYR 164 | LYS 159(PLP binding) | |||
| 1i1kA02 |
|
|
|
|
|
LYS 159;TYR 164 | LYS 159(PLP binding) | |||
| 1i1kB02 |
|
|
|
|
|
LYS 659;TYR 664 | LYS 659(PLP binding) | |||
| 1i1kC02 |
|
|
|
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|
LYS 1159;TYR 1164 | LYS 1159(PLP binding) | |||
| 1i1lA02 |
|
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|
LYS 159;TYR 164 | LYS 159(PLP binding) | |||
| 1i1lB02 |
|
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LYS 659;TYR 664 | LYS 659(PLP binding) | |||
| 1i1lC02 |
|
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|
LYS 1159;TYR 1164 | LYS 1159(PLP binding) | |||
| 1i1mA02 |
|
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|
LYS 159;TYR 164 | LYS 159(PLP binding) | |||
| 1i1mB02 |
|
|
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|
|
LYS 659;TYR 664 | LYS 659(PLP binding) | |||
| 1i1mC02 |
|
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|
|
|
LYS 1159;TYR 1164 | LYS 1159(PLP binding) | |||
| 1iydA02 |
|
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LYS 159;TYR 164 | LYS 159(PLP binding) | |||
| 1iydB02 |
|
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LYS 159;TYR 164 | LYS 159(PLP binding) | |||
| 1iydC02 |
|
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LYS 159;TYR 164 | LYS 159(PLP binding) | |||
| 1iyeA02 |
|
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LYS 159;TYR 164 | LYS 159(PLP binding) | |||
| 1iyeB02 |
|
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LYS 159;TYR 164 | LYS 159(PLP binding) | |||
| 1iyeC02 |
|
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LYS 159;TYR 164 | LYS 159(PLP binding) | |||
| 1ekfA02 |
|
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LYS 202;TYR 207 | LYS 202(PLP binding) | |||
| 1ekfB02 |
|
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LYS 202;TYR 207 | LYS 202(PLP binding) | |||
| 1ekpA02 |
|
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LYS 202;TYR 207 | LYS 202(PLP binding) | |||
| 1ekpB02 |
|
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|
LYS 202;TYR 207 | LYS 202(PLP binding) | |||
| 1ekvA02 |
|
|
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LYS 202;TYR 207 | LYS 202(PLP binding) | |||
| 1ekvB02 |
|
|
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|
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LYS 202;TYR 207 | LYS 202(PLP binding) | |||
| 1kt8A02 |
|
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|
LYS 202;TYR 207 | LYS 202(PLP binding) | |||
| 1kt8B02 |
|
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LYS 702;TYR 707 | LYS 702(PLP binding) | |||
| 1ktaA02 |
|
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LYS 202;TYR 207 | LYS 202(PLP binding) | |||
| 1ktaB02 |
|
|
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LYS 702;TYR 707 | LYS 702(PLP binding) | |||
| References for Catalytic Mechanism | ||
|---|---|---|
| References | Sections | No. of steps in catalysis |
|
[5]
|
p.111-112 | |
|
[6]
|
p.7459-7460 | |
|
[9]
|
p.11594-11599 | |
|
[10]
|
Scheme 2, Fig.7, p.3728-3730, p.3731-3733 | |
| References | |
|---|---|
| [1] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 2666406 |
| Journal | J Biochem (Tokyo) |
| Year | 1989 |
| Volume | 105 |
| Pages | 671-2 |
| Authors | Kamitori S, Odagaki Y, Inoue K, Kuramitsu S, Kagamiyama H, Matsuura Y, Higuchi T |
| Title | Crystallization and preliminary X-ray characterization of branched-chain amino acid aminotransferase from Escherichia coli. |
| Related PDB | |
| Related UniProtKB | |
| [2] | |
| Resource | |
| Comments | X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) |
| Medline ID | 97306043 |
| PubMed ID | 9163511 |
| Journal | J Biochem (Tokyo) |
| Year | 1997 |
| Volume | 121 |
| Pages | 637-41 |
| Authors | Okada K, Hirotsu K, Sato M, Hayashi H, Kagamiyama H |
| Title | Three-dimensional structure of Escherichia coli branched-chain amino acid aminotransferase at 2.5 A resolution. |
| Related PDB | 1a3g |
| Related UniProtKB | P0AB80 |
| [3] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 9914259 |
| Journal | Curr Opin Struct Biol |
| Year | 1998 |
| Volume | 8 |
| Pages | 759-69 |
| Authors | Jansonius JN |
| Title |
Structure, |
| Related PDB | |
| Related UniProtKB | |
| [4] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 10989422 |
| Journal | Methods Enzymol |
| Year | 2000 |
| Volume | 324 |
| Pages | 103-13 |
| Authors | Kagamiyama H, Hayashi H |
| Title | Branched-chain amino-acid aminotransferase of Escherichia coli. |
| Related PDB | |
| Related UniProtKB | |
| [5] | |
| Resource | |
| Comments | X-ray crystallography |
| Medline ID | |
| PubMed ID | 11264579 |
| Journal | Acta Crystallogr D Biol Crystallogr |
| Year | 2001 |
| Volume | 57 |
| Pages | 506-15 |
| Authors | Yennawar N, Dunbar J, Conway M, Hutson S, Farber G |
| Title | The structure of human mitochondrial branched-chain aminotransferase. |
| Related PDB | 1ekf 1ekp 1ekv |
| Related UniProtKB | |
| [6] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 11412098 |
| Journal | Biochemistry |
| Year | 2001 |
| Volume | 40 |
| Pages | 7453-63 |
| Authors | Okada K, Hirotsu K, Hayashi H, Kagamiyama H |
| Title | Structures of Escherichia coli branched-chain amino acid aminotransferase and its complexes with 4-methylvalerate and 2-methylleucine: induced fit and substrate recognition of the enzyme. |
| Related PDB | 1i1k 1i1l 1i1m |
| Related UniProtKB | |
| [7] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 11642362 |
| Journal | Prog Nucleic Acid Res Mol Biol |
| Year | 2001 |
| Volume | 70 |
| Pages | 175-206 |
| Authors | Hutson S |
| Title | Structure and function of branched chain aminotransferases. |
| Related PDB | |
| Related UniProtKB | |
| [8] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 12119021 |
| Journal | Biochemistry |
| Year | 2002 |
| Volume | 41 |
| Pages | 9070-8 |
| Authors | Conway ME, Yennawar N, Wallin R, Poole LB, Hutson SM |
| Title | Identification of a peroxide-sensitive redox switch at the CXXC motif in the human mitochondrial branched chain aminotransferase. |
| Related PDB | |
| Related UniProtKB | |
| [9] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 12269802 |
| Journal | Biochemistry |
| Year | 2002 |
| Volume | 41 |
| Pages | 11592-601 |
| Authors | Yennawar NH, Conway ME, Yennawar HP, Farber GK, Hutson SM |
| Title | Crystal structures of human mitochondrial branched chain aminotransferase reaction intermediates: ketimine and pyridoxamine phosphate forms. |
| Related PDB | 1kt8 1kta |
| Related UniProtKB | |
| [10] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 12667063 |
| Journal | Biochemistry |
| Year | 2003 |
| Volume | 42 |
| Pages | 3725-33 |
| Authors | Goto M, Miyahara I, Hayashi H, Kagamiyama H, Hirotsu K |
| Title | Crystal structures of branched-chain amino acid aminotransferase complexed with glutamate and glutarate: true reaction intermediate and double substrate recognition of the enzyme. |
| Related PDB | 1iyd 1iye |
| Related UniProtKB | |
| Comments |
|---|
|
This enzyme belongs to Type-VI PLP-dependent enzyme (see [3] & [5]).
According to the literature [10], (A) Formation of external aldimine (with amine group of the first substrate, (A1) The negative charges from phosphate group of PLP and alpha-carboxylate of the first substrate may deprotonate the nucleophile, (A2) The activated alpha-amino group of the first substrate makes a nucleophilic attack on the C4' atom of PLP (from the si-face side), (A3) Probably, (B) Isomerization (change in the position of double-bond). (B1) Lys159 acts as a general base to deprotonate the alpha-proton of the substrate bound to PLP, (B2) Lys159 acts as a general acid to protonate the C4' atom of the intermediate, (C) Schiff-base deforming (by hydration), (C1) Lys159 acts as a general base to activate a water (at the re-face side of cofactor). (C2) The activated water molecule makes a nucleophilic attack on the C-alpha atom of the substrate (from the re-face side), (C3) The lone pair of the new hydroxyl group makes a nucleophilic attack on the C4' atom, (D) Schiff-base forming (of PMP with carbonyl group of the second substrate, (E) Isomerization (change in the position of double-bond). (F) Formation of internal aldimine, |
| Created | Updated |
|---|---|
| 2004-03-18 | 2009-02-26 |