Purification, gene cloning, and characterization of γ-butyrobetainyl CoA synthetase fromAgrobacteriumsp. 525a

Autor:	Sayaka Takubo, Jiro Arima, Kazuma Okada, Hiroshi Fujimitsu, Isam A. Mohamed Ahmed, Nobuhiro Mori, Akiko Fukui, Akira Matsumoto
Rok vydání:	2016
Předmět:	0301 basic medicine Rhizobiaceae Agrobacterium Gene Expression Molecular cloning Applied Microbiology and Biotechnology Biochemistry Substrate Specificity Analytical Chemistry 03 medical and health sciences Bacterial Proteins Methylcrotonyl-CoA carboxylase Carnitine Coenzyme A Ligases Escherichia coli Amino Acid Sequence Cloning Molecular Overproduction Molecular Biology Soil Microbiology chemistry.chemical_classification Acyl-CoA synthetase Sequence Homology Amino Acid 030102 biochemistry & molecular biology biology Chemistry Organic Chemistry Protein primary structure General Medicine Hydrogen-Ion Concentration Agrobacterium sp biology.organism_classification Molecular biology Adenosine Diphosphate Betaine Kinetics 030104 developmental biology Enzyme Acyl Coenzyme A Sequence Alignment Biotechnology
Zdroj:	Bioscience, Biotechnology, and Biochemistry. 80:1536-1545
ISSN:	1347-6947 0916-8451
DOI:	10.1080/09168451.2016.1177447
Popis:	The report is the first of purification, overproduction, and characterization of a unique γ-butyrobetainyl CoA synthetase from soil-isolated Agrobacterium sp. 525a. The primary structure of the enzyme shares 70–95% identity with those of ATP-dependent microbial acyl-CoA synthetases of the Rhizobiaceae family. As distinctive characteristics of the enzyme of this study, ADP was released in the catalytic reaction process, whereas many acyl CoA synthetases are annotated as an AMP-forming enzyme. The apparent Km values for γ-butyrobetaine, CoA, and ATP were, respectively, 0.69, 0.02, and 0.24 mM.
Databáze:	OpenAIRE
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