type	Journal Article
authors	Kudou D, Yasuda E, Hirai Y, Tamura T, Inagaki K
title	Molecular cloning and characterization of l-methionine γ-lyase from Streptomyces avermitilis
journal	J Biosci Bioeng
Activity	4.4.1.11
Family	4.4.1.11
sel	selected
ui	25817696
year	(2015)
volume	120
number	4
pages	380-3
keywords	Elimination activity; Kinetic analysis; Phylogenetic analysis; Pyridoxal 5′-phosphate; Replacement activity; Streptomyces avermitilis; Substrate specificity; Thin-layer chromatography analysis; l-Methionine γ-lyase
abstract	A pyridoxal 5'-phosphate-dependent methionine γ-lyase (MGL) was cloned from Streptomyces avermitilis catalyzed the degradation of methionine to α-ketobutyrate, methanethiol, and ammonia. The sav7062 gene (1,242 bp) was corresponded to 413 amino acid residues with a molecular mass of 42,994 Da. The deduced amino acid sequence showed a high degree of similarity to those of other MGL enzymes. The sav7062 gene was overexpressed in Escherichia coli. The enzyme was purified to homogeneity and exhibited the MGL catalytic activities. We cloned the enzyme that has the MGL activity in Streptomyces for the first time.
last changed	2017/10/02 14:12