B6db activities : 5_1_1

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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.
	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
Family	5.1.1.21 (0)

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

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

last changed	2018/10/17 09:01

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