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Gene Review:

TTHA0940 - aminotransferase

Thermus thermophilus HB8

Hosono, A. et al., Goto, M. et al., Katsura, Y. et al., Arai, R. et al., Miyazaki, T. et al., et al.

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Disease relevance of TTHA0940

Crystal structures of glutamine:phenylpyruvate aminotransferase from Thermus thermophilus HB8: induced fit and substrate recognition [1].

High impact information on TTHA0940

Similarly, the glutamine:phenylpyruvate aminotransferase undergoes a large movement in part of the small domain to close the active site [1].
Aspartate aminotransferases (AspATs) from many species were classified into aminotransferase subgroups Ia and Ib [2].
In this study, a T. thermophilus gene encoding the enzyme that catalyses transamination of AAA was cloned as a mammalian kynurenine/AAA aminotransferase (Kat2) gene homologue [3].
A subfamily I aminotransferase gene homologue containing an open reading frame encoding 381 amino acid residues (Mr=42,271) has been identified in the process of the genome project of an extremely thermophilic bacterium, Thermus thermophilus HB8 [4].
Alignment of the predicted amino acid sequence using FASTA shows that this protein is a member of aminotransferase subfamily Igamma [4].

Chemical compound and disease context of TTHA0940

Protein TT0402 from Thermus thermophilus HB8 exhibits about 30-35% sequence identity with proteins belonging to subgroup IV in the aminotransferase family of the fold-type I pyridoxal 5'-phosphate (PLP)-dependent enzymes [5].

Biological context of TTHA0940

Since sequence homology analyses suggested that TTHA1620 was a pyridoxal 5'-phosphate-dependent enzyme, such as an aminotransferase, a cystathionine beta-lyase or a cystalysin, putative substrates were investigated [6].

Associations of TTHA0940 with chemical compounds

As the presence of aromatic amino acid:2-oxoglutarate aminotransferase [EC 2.6.1.57] has not been reported in T. thermophilus, this enzyme is expected to catalyze the last transamination step of phenylalanine and tyrosine biosynthesis [4].

References

Crystal structures of glutamine:phenylpyruvate aminotransferase from Thermus thermophilus HB8: induced fit and substrate recognition. Goto, M., Omi, R., Miyahara, I., Hosono, A., Mizuguchi, H., Hayashi, H., Kagamiyama, H., Hirotsu, K. J. Biol. Chem. (2004) [Pubmed]
Structures of Escherichia coli histidinol-phosphate aminotransferase and its complexes with histidinol-phosphate and N-(5'-phosphopyridoxyl)-L-glutamate: double substrate recognition of the enzyme. Haruyama, K., Nakai, T., Miyahara, I., Hirotsu, K., Mizuguchi, H., Hayashi, H., Kagamiyama, H. Biochemistry (2001) [Pubmed]
alpha-Aminoadipate aminotransferase from an extremely thermophilic bacterium, Thermus thermophilus. Miyazaki, T., Miyazaki, J., Yamane, H., Nishiyama, M. Microbiology (Reading, Engl.) (2004) [Pubmed]
Glutamine:phenylpyruvate aminotransferase from an extremely thermophilic bacterium, Thermus thermophilus HB8. Hosono, A., Mizuguchi, H., Hayashi, H., Goto, M., Miyahara, I., Hirotsu, K., Kagamiyama, H. J. Biochem. (2003) [Pubmed]
Crystal structure of a putative aspartate aminotransferase belonging to subgroup IV. Katsura, Y., Shirouzu, M., Yamaguchi, H., Ishitani, R., Nureki, O., Kuramitsu, S., Hayashi, H., Yokoyama, S. Proteins (2004) [Pubmed]
Conserved protein TTHA1554 from Thermus thermophilus HB8 binds to glutamine synthetase and cystathionine beta-lyase. Arai, R., Nishimoto, M., Toyama, M., Terada, T., Kuramitsu, S., Shirouzu, M., Yokoyama, S. Biochim. Biophys. Acta (2005) [Pubmed]

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