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2.6.1.18 a |
Activity |
2.6.1.18 |
Description |
Beta-alanine--pyruvate aminotransferase (family a) |
Notes |
The bacterial enzymes in this family are very similar to plant gamma-aminobutyrate--pyruvate aminotransferase (2.6.1.96, distinct from EC 2.6.1.19, which uses preferentially 2-oxoglutarate as an amino group acceptor) and to 2.6.1.113 (putrescine--pyruvate aminotransferase).
A sequence of "beta-alanine-pyruvate aminotransferase from rat" (accession n. BAA19549) is present in NCBI, but the sequence is essentially identical to that of mitochondrial alanine-glyoxylate aminotransferase 2 (2.1.6.44). |
PDB |
3A8U; |
PLP Fold Type |
I |
PLP-dependent Domain |
|
Number of sequences |
17 |
Sequences in seed alignment |
|
Reference sequence |
OAPT_PSEPU |
Domain interval |
35-390 |
Catalytic site |
288 K |
| |
References |
Wilding M, Peat TS, Newman J, Scott C (2016) A β-Alanine Catabolism Pathway Containing a Highly Promiscuous ω-Transaminase in the 12-Aminododecanate-Degrading Pseudomonas sp. Strain AAC Appl Environ Microbiol 82 3846-56. Yun, H.; Lim, S.; Cho, B.K.; Kim, B.G. (2004) omega-Amino acid:pyruvate transaminase from Alcaligenes denitrificans Y2k-2: a new catalyst for kinetic resolution of beta-amino acids and amines Appl Environ Microbiol 70 2529-34. Yonaha, K.; Nishie, M.; Aibara, S. (1992) The primary structure of omega-amino acid:pyruvate aminotransferase J Biol Chem 267 12506-10. Watanabe, N.
Sakabe, K.
Sakabe, N.
Higashi, T.
Sasaki, K.
Aibara, S.
Morita, Y.
Yonaha, K.
Toyama, S.
Fukutani, H. (1989) Crystal structure analysis of omega-amino acid:pyruvate aminotransferase with a newly developed Weissenberg camera and an imaging plate using synchrotron radiation J Biochem 105 1-3. Articles on 2.6.1.18.a |
last changed |
2020/02/17 12:14 |
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