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

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

doi:10.1016/j.jbiosc.2015.02.019

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

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

School of Agriculture

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

4 Citations (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 language	English
Pages (from-to)	380-383
Number of pages	4
Journal	Journal of Bioscience and Bioengineering
Volume	120
Issue number	4
DOIs	https://doi.org/10.1016/j.jbiosc.2015.02.019
Publication status	Published - Oct 1 2015

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
Bioengineering
Applied Microbiology and Biotechnology

Access to Document

10.1016/j.jbiosc.2015.02.019

Cite this

@article{ce2bd5761a7040dc91dea746bf5fa2e8,

title = "Molecular cloning and characterization of l-methionine γ-lyase from Streptomyces avermitilis",

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.",

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

author = "Daizou Kudou and Eri Yasuda and Yoshiyuki Hirai and Takashi Tamura and Kenji Inagaki",

note = "Publisher Copyright: {\textcopyright} 2015 The Society for Biotechnology, Japan.",

year = "2015",

month = oct,

day = "1",

doi = "10.1016/j.jbiosc.2015.02.019",

language = "English",

volume = "120",

pages = "380--383",

journal = "Journal of Bioscience and Bioengineering",

issn = "1389-1723",

publisher = "The Society for Biotechnology, Japan",

number = "4",

}

TY - JOUR

T1 - Molecular cloning and characterization of l-methionine γ-lyase from Streptomyces avermitilis

AU - Kudou, Daizou

AU - Yasuda, Eri

AU - Hirai, Yoshiyuki

AU - Tamura, Takashi

AU - Inagaki, Kenji

PY - 2015/10/1

Y1 - 2015/10/1

N2 - 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.

AB - 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.

KW - Elimination activity

KW - Kinetic analysis

KW - L-Methionine γ-lyase

KW - Phylogenetic analysis

KW - Pyridoxal 5'-phosphate

KW - Replacement activity

KW - Streptomyces avermitilis

KW - Substrate specificity

KW - Thin-layer chromatography analysis

UR - http://www.scopus.com/inward/record.url?scp=84940889865&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84940889865&partnerID=8YFLogxK

U2 - 10.1016/j.jbiosc.2015.02.019

DO - 10.1016/j.jbiosc.2015.02.019

M3 - Article

C2 - 25817696

AN - SCOPUS:84940889865

SN - 1389-1723

VL - 120

SP - 380

EP - 383

JO - Journal of Bioscience and Bioengineering

JF - Journal of Bioscience and Bioengineering

IS - 4

ER -

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

Abstract

Keywords

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this