Structural analysis of the L-methionine γ-lyase gene from Pseudomonas putida

Hiroyuki Inoue, Kenji Inagaki, Manabu Sugimoto, Nobuyoshi Esaki, Kenji Soda, Hidehiko Tanaka

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The gene encoding L-methionine γ-lyase from Pseudomonas putida was cloned and the primary structure of the enzyme was deduced from its nucleotide sequence. The L-methionine γ-lyase gene was expressed in Escherichia coli. The amino acid sequences of BrCN-digested peptides agreed with the corresponding parts of the L-methionine γ-lyase sequence determined from the gene structure. The polypeptide is composed of 398 amino acid residues with a calculated molecular weight of 42,626, corresponding to the subunit of the homotetrameric enzyme. The deduced amino acid sequence of L-methionine γ-lyase only showed extensive homology with other well known α,γ-elimination and/or γ-replacement pyridoxal 5'-phosphate-dependent enzymes, such as cystathionine γ-lyase, cystathionine γ-synthase, and O-acetylhomoserine O-acetylserine sulfhydrylase, that participate in the biosynthesis of sulfur amino acids. However, the deduced essential cysteine residue of L-methionine γ-lyase was not conserved in these enzymes. We confirmed the presence of a part of an open reading frame in the 3'-flanking region of the L-methionine γ-lyase gene, which showed high homology with the N-tenninal region of pyruvate dehydrogenase (lipoamide) from E. coli, suggesting that it participates in the degradative pathway for L-methionine together with L-methionine γ-lyase.

Original languageEnglish
Pages (from-to)1120-1125
Number of pages6
JournalJournal of biochemistry
Issue number5
Publication statusPublished - May 1995


  • L-methionine γ-lyase
  • Pseudomonas putida
  • Pyridoxal-P enzyme
  • Pyruvate dehydrogenase (lypoamide)

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology


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