Evidence that the putative α‐glucosidase of Thermotoga maritima MSB8 is a pNP α‐D‐glucuronopyranoside hydrolyzing α‐glucuronidase

FEBS Letters

Suresh, Cuddapah¹  Hayashi, Kiyoshi¹  Kitaoka, Motomitsu¹  Rus'd, Ahmed Abu¹ 

[1] Enzyme Laboratory, National Food Research Institute, 2-1-12 Kannondai, Tsukuba 305-8642, Ibaraki, Japan

关键词: Hyperthermophile;    p-Nitrophenyl α-D-glucuronopyranoside hydrolyzing α-glucuronidase;    Family 4 glycosyl hydrolase;    Thermotoga maritima;    pNP;    p-nitrophenol;    pNP-GUA;    p-nitrophenyl α-D-glucuronopyranoside;    pNP-Glc;    p-nitrophenyl α-D-glucopyranoside;    pNP-G6P;    p-nitrophenyl α-glucopyranoside-6-phosphate;    DTT;    dithiothreitol;   

DOI  :  10.1016/S0014-5793(02)02611-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The gene (agu) encoding p-nitrophenyl α-D-glucuronopyranoside (pNP-GUA) hydrolyzing α-glucuronidase of the hyperthermophilic bacterium Thermotoga maritima was cloned and expressed in Escherichia coli. The recombinant enzyme was purified and characterized. The gene previously designated as putative α-glucosidase was found to code for a protein that had no α-glucosidase activity. It showed a rare activity profile with its ability to hydrolyze pNP-GUA, an activity not known in the α-glucuronidases from microbial sources. This is the first report on the occurrence of an α-glucuronidase which belongs to the family 4 of glycosyl hydrolases.

【 授权许可】

Unknown