Purification, gene cloning, and characterization of γ-butyrobetainyl CoA synthetase from Agrobacterium sp. 525a-Reference-Cited by-同舟云学术

Purification, gene cloning, and characterization of γ-butyrobetainyl CoA synthetase from Agrobacterium sp. 525a

Published:2016-08-02 Issue:8 Volume:80 Page:1536-1545
ISSN:0916-8451
Container-title:Bioscience, Biotechnology, and Biochemistry
language:en
Short-container-title:

Author:

Fujimitsu Hiroshi¹²,Matsumoto Akira³,Takubo Sayaka³,Fukui Akiko³,Okada Kazuma³,Mohamed Ahmed Isam A⁴,Arima Jiro³,Mori Nobuhiro³

Affiliation:

1. United Graduate School of Agricultural Sciences, Tottori University, Tottori, Japan

2. Food Development Research Laboratory, Tottori Institute of Industrial Technology, Sakaiminato, Japan

3. Faculty of Agriculture, Department of Agricultural, Biological, and Environmental Sciences, Tottori University, Tottori, Japan

4. Department of Food Science and Nutrition, College of Food and Agricultural Sciences, King Saud University, Riyadh, KSA

Abstract

Abstract 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.

Publisher

Oxford University Press (OUP)

Subject

Organic Chemistry,Molecular Biology,Applied Microbiology and Biotechnology,General Medicine,Biochemistry,Analytical Chemistry,Biotechnology

Link

http://academic.oup.com/bbb/article-pdf/80/8/1536/36829623/bbb1536.pdf

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