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B6db activities: 2.6.1.57

2.6.1.57
Description Aromatic amino acid transaminase.
Catalyzed reaction An aromatic amino acid + 2-oxoglutarate = an aromatic oxo acid + L-glutamate.
Cofactor Pyridoxal-phosphate.
Comments -!- L-methionine can also act as donor, more slowly.
-!- Oxaloacetate can act as acceptor.
-!- Controlled proteolysis converts the enzyme to EC 2.6.1.1. include 2.6.1.5
Enzymes with this activity are strictly related to aspartate aminotransferase enzymes (EC 2.6.1.1).

Sequences in family a are most similar to aspartate aminotransferases in families 2.6.1.1_a and 2.6.1.1_c.

Sequences in family b are most similar to enzymes belonging to family 2.6.1.1_b.

A yeast gene encoding a transaminase with broad substrate specificity is sometimes annotated as aromatic aminoacid aminotransferase, but it apparently prefers 2-aminoadipate as a substrate and is included in family 2.6.1.39_a.

Prosite PROSITE; PDOC00098;
PDB 1AY4; 3TAT; 1DJU; 1GD9;
Organisms -Bacteria -Archea -Fungi -Metazoa
 

Family 

2.6.1.57_a (13) 2.6.1.57_b (15)
 
Links Enzyme (activities) 2.6.1.57
BRENDA (activities) 2.6.1.57
KEGG (pathways) 2.6.1.57
PLPMDB (PLP mutants) 2.6.1.57
 
References
 Matsui, I.; Matsui, E.; Sakai, Y.; Kikuchi, H.; Kawarabayasi, Y.; Ura, H.; Kawaguchi, S.; Kuramitsu, S.; Harata, K. (2000) The molecular structure of hyperthermostable aromatic aminotransferase with novel substrate specificity from Pyrococcus horikoshii J Biol Chem 275 4871-9.

 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.

 Rijnen, L.; Bonneau, S.; Yvon, M. (1999) Genetic characterization of the major lactococcal aromatic aminotransferase and its involvement in conversion of amino acids to aroma compounds Appl Environ Microbiol 65 4873-80..

 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
 
last changed 2009/05/07 14:28

B6db activities