Purification of bacterial l-methionine γ-lyase

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

doi:10.1016/0003-2697(84)90832-7

Purification of bacterial l-methionine γ-lyase

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

ENG - Biomolecular Engineering

Research output: Contribution to journal › Article › peer-review

66 Citations (Scopus)

Abstract

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 language	English
Pages (from-to)	421-424
Number of pages	4
Journal	Analytical Biochemistry
Volume	138
Issue number	2
DOIs	https://doi.org/10.1016/0003-2697(84)90832-7
Publication status	Published - 1984 May 1

Keywords

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

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title = "Purification of bacterial l-methionine γ-lyase",

abstract = "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).",

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author = "Toru Nakayama and Nobuyoshi Esaki and Kunio Sugie and Beresov, {Temir T.} and Hidehiko Tanaka and Kenji Soda",

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AU - Nakayama, Toru

AU - Esaki, Nobuyoshi

AU - Sugie, Kunio

AU - Beresov, Temir T.

AU - Tanaka, Hidehiko

AU - Soda, Kenji

PY - 1984/5/1

Y1 - 1984/5/1

N2 - 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).

AB - 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).

KW - bacterial enzyme

KW - enzyme purification

KW - methionine γ-lyase

KW - sulfur amino acids

KW - vitamin B enzyme

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Purification of bacterial l-methionine γ-lyase

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