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

Paper ID Volume ID Publish Year Pages File Format Full-Text
20147 43160 2015 4 PDF Available
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
Pyridoxal 5′-phosphate; l-Methionine γ-lyase; Streptomyces avermitilis; Elimination activity; Replacement activity; Substrate specificity; Thin-layer chromatography analysis; Kinetic analysis; Phylogenetic analysis
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Molecular cloning and characterization of l-methionine γ-lyase from Streptomyces avermitilis
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Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Bioscience and Bioengineering - Volume 120, Issue 4, October 2015, Pages 380–383
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
Online Support
Any Questions? feel free to contact us