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O-acetylhomoserine sulfhydrylase from Clostridium novyi. Cloning, expression of the gene and characterization of the enzyme
- Source :
- Protein expression and purification. 180
- Publication Year :
- 2020
-
Abstract
- The gene NT01CX_1210 of pathogenic bacterium Clostridium novyi annotated as encoding O-acetylhomoserine sulfhydrylase was cloned and expressed in Escherichia coli. The gene product having O-acetylhomoserine sulfhydrylase activity was purified to homogeneity. The protein showed molecular mass of approximately 184 kDa for the native form and 46 kDa for the subunit. The enzyme catalyzes the γ-substitution reaction of O-acetylhomoserine with maximum activity at pH 7.5. Analysis of C. novyi genome allowed us to suggest that there is only one way for the synthesis of l -methionine in the bacterium. The data obtained may provide the basis for further study of the role of OAHS in Clostridium bacteria and an ascertainment of its mechanism.
- Subjects :
- 0106 biological sciences
Protein subunit
Carbon-Oxygen Lyases
Gene Expression
medicine.disease_cause
01 natural sciences
Gene product
03 medical and health sciences
Bacterial Proteins
010608 biotechnology
medicine
Cloning, Molecular
Escherichia coli
Gene
030304 developmental biology
chemistry.chemical_classification
Clostridium
0303 health sciences
biology
Molecular mass
Chemistry
biology.organism_classification
Clostridium novyi
Recombinant Proteins
Enzyme
Biochemistry
Bacteria
Biotechnology
Subjects
Details
- ISSN :
- 10960279
- Volume :
- 180
- Database :
- OpenAIRE
- Journal :
- Protein expression and purification
- Accession number :
- edsair.doi.dedup.....512bf3af6d510ea48d52f7ffaf2d3e92