Purification of bacterial l-methionine γ-lyase

Toru Nakayama, Nobuyoshi Esaki, Kunio Sugie, Temir T. Beresov, Hidehiko Tanaka, Kenji Soda

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66 Citations (Scopus)


A rapid procedure for the purification of l-methionine γ-lyase from Pseudomonas putida ICR 3460 by DEAE-TOYOPEARL 650M and DEAE-Sephadex A-50 column chromatography is presented. The enzyme was purified with an average yield of 75% and showed about 10-fold higher specific activity than the enzyme from P. putida (=P. ovalis) IFO 3738 reported previously (H. Tanaka, N. Esaki, and K. Soda (1976) FEBS Lett. 66, 307-311). The present enzyme has a molecular weight of about 172,000 and consists of four subunits with identical molecular weights (43,000). It shows the typical absorption spectrum of pyridoxal enzyme with maxima at 278 and 420 nm, and contains 4 mol of pyridoxal 5′-phosphate per mole of enzyme. The enzyme has a multicatalytic function similar to the enzyme of P. putida IFO 3738 (K. Soda, H. Tanaka, and N. Esaki (1983) Trends Biochem. Sci. 8, 214-217).

Original languageEnglish
Pages (from-to)421-424
Number of pages4
JournalAnalytical Biochemistry
Issue number2
Publication statusPublished - 1984 May 1


  • bacterial enzyme
  • enzyme purification
  • methionine γ-lyase
  • sulfur amino acids
  • vitamin B enzyme


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