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B6db families: 2.6.1.57.a

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, -methylphenylalanine transaminase activity (EC 2.6.1.107).

PDB 1AY4;4RKC;
PLP Fold Type I
PLP-dependent Domain
Domain alignment
Domain hmm
Fold type I

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

B6db families