极端嗜盐古菌日本盐杆菌 GlgC 同源蛋白的特性研究。

Characterization of a GlgC homolog from extremely halophilic archaeon Haloarcula japonica.

机构信息

School of Life Science and Technology, Tokyo Institute of Technology, Midori-ku, Yokohama, Japan.

National Institute of Technology, Numazu College, Numazu, Shizuoka, Japan.

出版信息

Biosci Biotechnol Biochem. 2021 May 25;85(6):1441-1447. doi: 10.1093/bbb/zbab050.

DOI:10.1093/bbb/zbab050

PMID:33749776

Abstract

Glycogen synthesis in bacteria is mainly organized by the products of glgB, glgC, and glgA genes comprising the widely known glg operon. On the genome of extremely halophilic archaeon Haloarcula japonica, there was a gene cluster analogous to the bacterial glg operon. In this study, we focused on a GlgC homolog of Ha. japonica, and its recombinant enzyme was prepared and characterized. The enzyme showed highest activity toward GTP and glucose-1-phosphate as substrates in the presence of 2.6 m KCl and predicted to be work as "GDP-glucose pyrophosphorylase" in Ha. japonica.

摘要

在细菌中，糖原的合成主要由 glgB、glgC 和 glgA 基因的产物组织，这些基因构成了广为人知的 glg 操纵子。在极端嗜盐古菌日本盐球菌的基因组中，有一个类似于细菌 glg 操纵子的基因簇。在本研究中，我们专注于日本盐球菌的 GlgC 同源物，并制备和表征了其重组酶。该酶在 2.6 m KCl 存在下以 GTP 和葡萄糖-1-磷酸作为底物表现出最高的活性，预测在日本盐球菌中作为“GDP-葡萄糖焦磷酸化酶”发挥作用。