1cb2
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(New page: 200px<br /> <applet load="1cb2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cb2, resolution 2.0Å" /> '''CELLOBIOHYDROLASE II...)
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Revision as of 19:20, 29 October 2007
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CELLOBIOHYDROLASE II, CATALYTIC DOMAIN, MUTANT Y169F
Overview
Trichoderma reesei cellobiohydrolase II (CBHII) is an exoglucanase, cleaving primarily cellobiose units from the non-reducing end of cellulose, chains. The beta-1,4 glycosidic bond is cleaved by acid catalysis with an, aspartic acid, D221, as the likely proton donor, and another aspartate, D175, probably ensuring its protonation and stabilizing charged reaction, intermediates. The catalytic base has not yet been identified, experimentally. The refined crystal structure of CBHII also shows a, tyrosine residue, Y169, located close enough to the scissile bond to be, involved in catalysis. The role of this residue has been studied by, introducing a mutation Y169F, and analysing the kinetic and binding, behavior of the mutated CBHII. The crystal structure of the mutated enzyme, was determined ... [(full description)]
About this Structure
1CB2 is a [Single protein] structure of sequence from [Trichoderma reesei] with NAG and MAN as [ligands]. Active as [[1]], with EC number [3.2.1.91]. Full crystallographic information is available from [OCA].
Reference
The active site of Trichoderma reesei cellobiohydrolase II: the role of tyrosine 169., Koivula A, Reinikainen T, Ruohonen L, Valkeajarvi A, Claeyssens M, Teleman O, Kleywegt GJ, Szardenings M, Rouvinen J, Jones TA, Teeri TT, Protein Eng. 1996 Aug;9(8):691-9. PMID:8875646
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