Journal of Bioscience and Bioengineering, Vol.120, No.4, 380-383, 2015
Molecular cloning and characterization of L-methionine gamma-lyase from Streptomyces avermitilis
A pyridoxal 5'-phosphate-dependent methionine gamma-lyase (MGL) was cloned from Streptomyces avermitilis catalyzed the degradation of methionine to alpha-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. (C) 2015, The Society for Biotechnology, Japan. All rights reserved.
Keywords:Pyridoxal 5'-phosphate;L-Methionine gamma-lyase;Streptomyces avermitilis;Elimination activity;Replacement activity;Substrate specificity;Thin-layer chromatography analysis;Kinetic analysis;Phylogenetic analysis