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.
authors.affiliation: Department of Biofunctional Chemistry, Graduate School of Environmental and Life Science, Okayama University, Tsushima-naka 1-1-1, Kita-ku, Okayama-shi, Okayama 700-8530, Japan. Electronic address: daizo.kudo@hb.nagase.co.jp.
authors.forename: Daizou
authors.initials: D
authors.lastname: Kudou
authors.affiliation: Department of Biofunctional Chemistry, Graduate School of Environmental and Life Science, Okayama University, Tsushima-naka 1-1-1, Kita-ku, Okayama-shi, Okayama 700-8530, Japan. Electronic address: ag422114@s.okayama-u.ac.jp.
authors.forename: Eri
authors.initials: E
authors.lastname: Yasuda
authors.affiliation: Department of Biofunctional Chemistry, Graduate School of Environmental and Life Science, Okayama University, Tsushima-naka 1-1-1, Kita-ku, Okayama-shi, Okayama 700-8530, Japan. Electronic address: y_hirai@tacr.co.jp.
authors.forename: Yoshiyuki
authors.initials: Y
authors.lastname: Hirai
authors.affiliation: Department of Biofunctional Chemistry, Graduate School of Environmental and Life Science, Okayama University, Tsushima-naka 1-1-1, Kita-ku, Okayama-shi, Okayama 700-8530, Japan. Electronic address: tktamura@okayama-u.ac.jp.
authors.forename: Takashi
authors.initials: T
authors.lastname: Tamura
authors.affiliation: Department of Biofunctional Chemistry, Graduate School of Environmental and Life Science, Okayama University, Tsushima-naka 1-1-1, Kita-ku, Okayama-shi, Okayama 700-8530, Japan. Electronic address: kinagaki@okayama-u.ac.jp.
authors.forename: Kenji
authors.initials: K
authors.lastname: Inagaki
mesh_terms: D000595:Amino Acid Sequence; D000641:Ammonia / Q000378:metabolism; D055162:Biocatalysis; D002087:Butyrates / Q000378:metabolism; D013437:Carbon-Sulfur Lyases / Q000737:chemistry / Q000235:genetics* / Q000302:isolation & purification / Q000378:metabolism*; D003001:Cloning, Molecular; D004926:Escherichia coli / Q000235:genetics; D008715:Methionine / Q000378:metabolism; D008969:Molecular Sequence Data; D008970:Molecular Weight; D013302:Streptomyces / Q000201:enzymology* / Q000235:genetics; D013438:Sulfhydryl Compounds / Q000378:metabolism
chemical_list: D002087:Butyrates; D013438:Sulfhydryl Compounds; C005231:methylmercaptan; C005087:alpha-ketobutyric acid; D000641:Ammonia; D008715:Methionine; D013437:Carbon-Sulfur Lyases; C021558:L-methionine gamma-lyase
keywords: Elimination activity; Kinetic analysis; Phylogenetic analysis; Pyridoxal 5′-phosphate; Replacement activity; Streptomyces avermitilis; Substrate specificity; Thin-layer chromatography analysis; l-Methionine γ-lyase