在真菌和芽孢杆菌糖苷酶中发现的纤维单胞菌葡聚糖酶催化结构域的同源物。
Homologues of catalytic domains of Cellulomonas glucanases found in fungal and Bacillus glycosidases.
作者信息
West C A, Elzanowski A, Yeh L S, Barker W C
机构信息
Protein Identification Resource, National Biomedical Research Foundation, Georgetown University Medical Center, Washington, DC 20007.
出版信息
FEMS Microbiol Lett. 1989 May;50(1-2):167-72. doi: 10.1016/0378-1097(89)90479-5.
We demonstrate homology between the catalytic domains of exoglucanase (1,4-beta-D-glucan cellobiohydrolase, EC 3.2.1.91) from Cellulomonas fimi and those of endoxylanases (1,4-beta-D-xylan xylanohydrolases, EC 3.2.1.8) from Bacillus sp. strain C-125 and the fungus Cryptococcus albidus; and between the catalytic domains of endoglucanase (1,4-(1,3:1,4)-beta-D-glucan 4-glucanohydrolase, EC 3.2.1.4) from Cellulomonas fimi and exoglucanase II from Trichoderma reesei. These five enzymes apparently evolved by reshuffling of two catalytic domains and several substrate-binding domains.
我们证明了纤维单胞菌（Cellulomonas fimi）的外切葡聚糖酶（1,4-β-D-葡聚糖纤维二糖水解酶，EC 3.2.1.91）的催化结构域与芽孢杆菌属（Bacillus sp.）菌株C-125和真菌浅白隐球酵母（Cryptococcus albidus）的内切木聚糖酶（1,4-β-D-木聚糖木聚糖水解酶，EC 3.2.1.8）的催化结构域之间具有同源性；以及纤维单胞菌的内切葡聚糖酶（1,4-(1,3:1,4)-β-D-葡聚糖4-葡聚糖水解酶，EC 3.2.1.4）的催化结构域与里氏木霉（Trichoderma reesei）的外切葡聚糖酶II之间具有同源性。这五种酶显然是通过两个催化结构域和几个底物结合结构域的重排而进化的。
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