ENZYMES IN OLIGOSACCHARIDE SYNTHESIS - ACTIVE-DOMAIN OVERPRODUCTION, SPECIFICITY STUDY, AND SYNTHETIC USE OF AN ALPHA-1,2-MANNOSYLTRANSFERASE WITH REGENERATION OF GDP-MAN

被引：53

作者：

WANG, P ^{[1
]}

SHEN, GJ ^{[1
]}

WANG, YF ^{[1
]}

ICHIKAWA, Y ^{[1
]}

WONG, CH ^{[1
]}

机构：

[1] Scripps Res Inst, DEPT CHEM, 10666 N TORREY PINES RD, LA JOLLA, CA 92037 USA

来源：

JOURNAL OF ORGANIC CHEMISTRY | 1993年 / 58卷 / 15期

关键词：

D O I：

10.1021/jo00067a035

中图分类号：

O62 [有机化学];

学科分类号：

070303 [有机化学]; 081704 [应用化学];

摘要：

The catalytic domain of a membrane-bound alpha-1,2-mannosyltransferase (ManT) from yeast has been overexpressed in E. coli, at a level of approximately 0.7-0.8 units per L with a specific activity of about 1 U/mg (based on a-methyl mannoside) after purification. The E. coli strain has been deposited in ATCC (#77379) and will be available to the public. The isolated ManT is stable in 30% methanol or 20% acetone. It accepts mannose, mannobiose, and O-mannosylglycopeptides as acceptors. A multiple enzyme system with in situ regeneration of GDP-mannose suitable for large-scale synthesis of mannosides and mannosyl glycopeptides has been developed.

引用

页码：3985 / 3990

页数：6

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