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 journalArticle

1 Citation (Scopus)

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.

Original languageEnglish
Pages (from-to)380-383
Number of pages4
JournalJournal of Bioscience and Bioengineering
Volume120
Issue number4
DOIs
Publication statusPublished - Oct 1 2015

Fingerprint

Lyases
Cloning
Streptomyces
Molecular Cloning
Methionine
Enzymes
Amino acids
Genes
Amino Acids
Pyridoxal Phosphate
Molecular mass
Ammonia
Escherichia coli
Amino Acid Sequence
Catalyst activity
Phosphates
Degradation

Keywords

  • 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
  • Applied Microbiology and Biotechnology
  • Bioengineering

Cite this

Molecular cloning and characterization of l-methionine γ-lyase from Streptomyces avermitilis. / Kudou, Daizou; Yasuda, Eri; Hirai, Yoshiyuki; Tamura, Takashi; Inagaki, Kenji.

In: Journal of Bioscience and Bioengineering, Vol. 120, No. 4, 01.10.2015, p. 380-383.

Research output: Contribution to journalArticle

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