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5.1.1.21 |
Description |
Isoleucine 2-epimerase |
Alternative names |
BCAA racemase |
Catalyzed reaction |
L-isoleucine = D-allo-isoleucine |
Cofactor |
Pyridoxal-phosphate. |
Comments |
A pyridoxal phosphate protein. The enzyme, characterized from the bacterium Lactobacillus buchneri, specifically catalyses racemization of nonpolar amino acids at the C-2 position. |
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The enzyme catalyzed the racemization of a broad spectrum of nonpolar amino acids. In particular, it catalyzed at high rates the epimerization of l-isoleucine to d-allo-isoleucine and d-allo-isoleucine to l-isoleucine. |
PDB |
4YSN; |
Organisms |
-Eubacteria |
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Family |
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Links |
Enzyme (activities) 5.1.1.21
BRENDA (activities) 5.1.1.21
KEGG (pathways) 5.1.1.21
PLPMDB (PLP mutants) 5.1.1.21
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References |
Awad R, Gans P, Reiser JB (2017) Structural insights into the substrate recognition and reaction specificity of the PLP-dependent fold-type I isoleucine 2-epimerase from Lactobacillus buchneri Biochimie 137 165-173. Hayashi J, Mutaguchi Y, Minemura Y, Nakagawa N, Yoneda K, Ohmori T, Ohshima T, Sakuraba H (2017) Crystal structure of the novel amino-acid racemase isoleucine 2-epimerase from Lactobacillus buchneri Acta Crystallogr D Struct Biol 73 428-437. Mutaguchi Y, Ohmori T, Wakamatsu T, Doi K, Ohshima T. (2013) Identification, purification, and characterization of a novel amino acid racemase, isoleucine 2-epimerase, from Lactobacillus species. J Bacteriol. 195 5207-15. Articles on 5.1.1.21 |
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last changed |
2018/10/17 09:01 |
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