Suresh Cuddapah, Rus'd Ahmed Abu, Kitaoka Motomitsu, Hayashi Kiyoshi
Enzyme Laboratory, National Food Research Institute, Ibaraki, Tsukuba, Japan.
FEBS Lett. 2002 Apr 24;517(1-3):159-62. doi: 10.1016/s0014-5793(02)02611-x.
The gene (agu) encoding p-nitrophenyl alpha-D-glucuronopyranoside (pNP-GUA) hydrolyzing alpha-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 alpha-glucosidase was found to code for a protein that had no alpha-glucosidase activity. It showed a rare activity profile with its ability to hydrolyze pNP-GUA, an activity not known in the alpha-glucuronidases from microbial sources. This is the first report on the occurrence of an alpha-glucuronidase which belongs to the family 4 of glycosyl hydrolases.
编码嗜热栖热菌（Thermotoga maritima）对α-D-葡糖醛酸对硝基苯吡喃糖苷（pNP-GUA）具有水解活性的α-葡糖醛酸酶的基因（agu）被克隆并在大肠杆菌中表达。对重组酶进行了纯化和特性分析。先前被指定为假定α-葡糖苷酶的基因被发现编码一种不具有α-葡糖苷酶活性的蛋白质。它表现出一种罕见的活性特征，即具有水解pNP-GUA的能力，这种活性在微生物来源的α-葡糖醛酸酶中并不为人所知。这是关于属于糖基水解酶家族4的α-葡糖醛酸酶存在的首次报道。
Zotero 插件