1ojk: Difference between revisions

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[[Category: hydrolase]]
[[Category: hydrolase]]


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Revision as of 16:51, 30 October 2007

File:1ojk.gif


1ojk, resolution 1.50Å

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ANATOMY OF GLYCOSYNTHESIS: STRUCTURE AND KINETICS OF THE HUMICOLA INSOLENS CEL7BE197A AND E197S GLYCOSYNTHASE MUTANTS

OverviewOverview

The formation of glycoconjugates and oligosaccharides remains one of the, most challenging chemical syntheses. Chemo-enzymatic routes using, retaining glycosidases have been successfully harnessed but require tight, kinetic or thermodynamic control. "Glycosynthases," specifically, engineered glycosidases that catalyze the formation of glycosidic bonds, from glycosyl donor and acceptor alcohol, are an emerging range of, synthetic tools in which catalytic nucleophile mutants are harnessed, together with glycosyl fluoride donors to generate powerful and versatile, catalysts. Here we present the structural and kinetic dissection of the, Humicola insolens Cel7B glycosynthases in which the nucleophile of the, wild-type enzyme is mutated to alanine and serine (E197A and E197S). 3-D, structures ... [(full description)]

About this StructureAbout this Structure

1OJK is a [Single protein] structure of sequence from [Humicola insolens] with NAG and GOL as [ligands]. Active as [Cellulase], with EC number [3.2.1.4]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

ReferenceReference

Anatomy of glycosynthesis: structure and kinetics of the Humicola insolens Cel7B E197A and E197S glycosynthase mutants., Ducros VM, Tarling CA, Zechel DL, Brzozowski AM, Frandsen TP, von Ossowski I, Schulein M, Withers SG, Davies GJ, Chem Biol. 2003 Jul;10(7):619-28. PMID:12890535

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