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r-amine:pyruvate_aminotransferase |
Description |
(R)-amine:pyruvate aminotransferase (2.6.1.-) |
Catalyzed reaction |
(R)-2-amine + pyruvate = 2- oxo-compound + D-alanine |
Cofactor |
Pyridoxal-phosphate. |
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A novel (R)-amine transaminase, which catalyzed (R)-enantioselective transamination of chiral amine, was purified to homogeneity from Arthrobacter sp. KNK168. The enzyme catalyzed transamination between amines and pyruvate stereo-specifically. The deduced amino acid sequence was found to be homologous to those of the aminotransferases belonging to fold class IV of pyridoxal-5'-phosphate-dependent enzymes, such as branched-chain amino acid aminotransferases. |
Organisms |
-Eubacteria |
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Family |
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Links |
Enzyme (activities) r-amine:pyruvate_aminotransferase
BRENDA (activities) r-amine:pyruvate_aminotransferase
KEGG (pathways) r-amine:pyruvate_aminotransferase
PLPMDB (PLP mutants) r-amine:pyruvate_aminotransferase
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References |
Łyskowski A, Gruber C, Steinkellner G, Schürmann M, Schwab H, Gruber K, Steiner K. (2014) Crystal structure of an (R)-selective ω-transaminase from Aspergillus terreus. PLoS One. 9 e87350. Iwasaki A, Matsumoto K, Hasegawa J, Yasohara Y. (2012) A novel transaminase, (R)-amine:pyruvate aminotransferase, from Arthrobacter sp. KNK168 (FERM BP-5228): purification, characterization, and gene cloning. Appl Microbiol Biotechnol. 93 1563-73. Articles on r-amine.pyruvate.aminotransferase |
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last changed |
2014/04/16 13:32 |
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