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2.6.1.57 a |
Activity |
2.6.1.57 |
Description |
Aromatic amino acid transaminase (family a) |
Notes |
Sequences in this family come from Gram- bacteria, and are strict homologs of aspartate aminotransferase enzymes belonging to families 2.6.1.1_a and 2.6.1.1_c.
The enzyme from E. coli was also shown to possess, in vitro, ß-methylphenylalanine transaminase activity (EC 2.6.1.107). |
PDB |
1AY4;4RKC; |
PLP Fold Type |
I |
PLP-dependent Domain |
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Number of sequences |
14 |
Sequences in seed alignment |
|
Reference sequence |
TYRB_ECOLI |
Domain interval |
26-393 |
Catalytic site |
247 K |
| |
References |
Bujacz A, Rutkiewicz-Krotewicz M, Nowakowska-Sapota K, Turkiewicz M (2015) Crystal structure and enzymatic properties of a broad substrate-specificity psychrophilic aminotransferase from the Antarctic soil bacterium Psychrobacter sp. B6
Acta Crystallogr D Biol Crystallogr 71 632-45. Heilbronn, J.; Wilson, J.; Berger, B.J. (1999) Tyrosine aminotransferase catalyzes the final step of methionine recycling in Klebsiella pneumoniae
J Bacteriol 181 1739-47. Gu, W.; Song, J.; Bonner, C.A.; Xie, G.; Jensen, R.A.
(1998) PhhC is an essential aminotransferase for aromatic amino acid catabolism in Pseudomonas aeruginosa Microbiology 144 3127-34. Oue, S.; Okamoto, A.; Nakai, Y.; Nakahira, M.; Shibatani, T.; Hayashi, H.; Kagamiyama, H. (1997) Paracoccus denitrificans aromatic amino acid aminotransferase: a model enzyme for the study of dual substrate recognition mechanism J Biochem (Tokyo) 121 161-71. Hayashi, H.; Inoue, K.; Nagata, T.; Kuramitsu, S.; Kagamiyama, H. (1993) Escherichia coli aromatic amino acid aminotransferase: characterization and comparison with aspartate aminotransferase Biochemistry 32 12229-39. Articles on 2.6.1.57.a |
last changed |
2017/11/15 10:06 |
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