Molecular cloning and characterization of l-methionine γ-lyase from Streptomyces avermitilis
| Autor: | Daizou Kudou, Eri Yasuda, Kenji Inagaki, Takashi Tamura, Yoshiyuki Hirai |
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| Rok vydání: | 2014 |
| Předmět: |
Molecular Sequence Data
Bioengineering Molecular cloning Applied Microbiology and Biotechnology Streptomyces chemistry.chemical_compound Methionine Ammonia Escherichia coli Amino Acid Sequence Sulfhydryl Compounds Cloning Molecular Peptide sequence chemistry.chemical_classification biology Molecular mass biology.organism_classification Lyase Molecular Weight Butyrates Carbon-Sulfur Lyases Enzyme chemistry Biochemistry Biocatalysis Streptomyces avermitilis Biotechnology |
| Zdroj: | Journal of bioscience and bioengineering. 120(4) |
| ISSN: | 1347-4421 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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