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B6db references: 25817696

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
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

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