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tuzn1299 |
| Description |
Branched chain amino acid--pyruvate transaminase (low-specificity) (2.6.1.-) |
| Alternative names |
TUZN1299 (gene name);
VMUT0738 (gene name); |
| Catalyzed reaction |
4-methyl-2-oxovalerate+alanine = leucine+ pyruvate |
| Cofactor |
Pyridoxal-phosphate |
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TUZN1299 was found to be highly active toward branched-chain amino acids (BCAAs), positively charged amino acids, l-methionine, l-threonine, l-homoserine, l-glutamine, as well as toward 2-oxobutyrate and keto analogs of BCAAs, whereas l-glutamate and α-ketoglutarate were not converted in the overall reaction. (This is a striking difference with respect to classic BCAATs, grouped in family 2.6.1.42_a) |
| PDB |
5CE8:; |
| Organisms |
-Archea |
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Family |
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| Links |
Enzyme (activities) tuzn1299
BRENDA (activities) tuzn1299
KEGG (pathways) tuzn1299
PLPMDB (PLP mutants) tuzn1299
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| References |
Stekhanova TN, Rakitin AL, Mardanov AV, Bezsudnova EY, Popov VO (2017) A Novel highly thermostable branched-chain amino acid aminotransferase from the crenarchaeon Vulcanisaeta moutnovskia Enzyme Microb Technol 96 127-134. Bezsudnova EY, Stekhanova TN, Suplatov DA, Mardanov AV (2016) Experimental and computational studies on the unusual substrate specificity of branched-chain amino acid aminotransferase from Thermoproteus uzoniensis Arch. Biochem. Biophys. 607 27-36. Boyko KM, Stekhanova TN, Nikolaeva AY, Mardanov AV, Rakitin AL, Ravin NV, Bezsudnova EY, Popov VO (2016) First structure of archaeal branched-chain amino acid aminotransferase from Thermoproteus uzoniensis specific for L-amino acids and R-amines Extremophiles 20 215-25. |
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| last changed |
2019/06/20 13:28 |
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