Molecular cloning and characterization of l-methionine γ-lyase from Streptomyces avermitilis

Daizou Kudou, Eri Yasuda, Yoshiyuki Hirai, Takashi Tamura, Kenji Inagaki

Research output: Contribution to journalArticlepeer-review

4 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)380-383
Number of pages4
JournalJournal of Bioscience and Bioengineering
Issue number4
Publication statusPublished - Oct 1 2015


  • Elimination activity
  • Kinetic analysis
  • L-Methionine γ-lyase
  • Phylogenetic analysis
  • Pyridoxal 5'-phosphate
  • Replacement activity
  • Streptomyces avermitilis
  • Substrate specificity
  • Thin-layer chromatography analysis

ASJC Scopus subject areas

  • Biotechnology
  • Bioengineering
  • Applied Microbiology and Biotechnology


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