2his
From Proteopedia
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==About this Structure== | ==About this Structure== | ||
| - | 2HIS is a | + | 2HIS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Cellulomonas_fimi Cellulomonas fimi]. Active as [http://en.wikipedia.org/wiki/Cellulose_1,4-beta-cellobiosidase Cellulose 1,4-beta-cellobiosidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.91 3.2.1.91] Structure known Active Site: NUC. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2HIS OCA]. |
==Reference== | ==Reference== | ||
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[[Category: xylanase/cellulase]] | [[Category: xylanase/cellulase]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 5 13:18:13 2007'' |
Revision as of 11:12, 5 November 2007
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CELLULOMONAS FIMI XYLANASE/CELLULASE DOUBLE MUTANT E127A/H205N WITH COVALENT CELLOBIOSE
Overview
The catalytic mechanism of 'retaining' beta-glycosidases has been the, subject of considerable interest and debate for many years. The, visualization of a covalent glycosyl enzyme intermediate by X-ray, crystallography was first accomplished with a saccharide substrate, substituted with fluorine at its 2-position. The structure implicated, major roles for residue His 205 and for the 2-hydroxyl position of the, proximal saccharide in binding and catalysis. Here we have studied the, kinetic behavior of various His 205 mutants. One of these mutants, a, double mutant H205N/E127A, has been used to stabilize a covalent, glycosyl-enzyme intermediate involving an unsubstituted sugar, permitting, crystallographic analysis of the interactions between its 2-hydroxyl group, and the enzyme.
About this Structure
2HIS is a Single protein structure of sequence from Cellulomonas fimi. Active as Cellulose 1,4-beta-cellobiosidase, with EC number 3.2.1.91 Structure known Active Site: NUC. Full crystallographic information is available from OCA.
Reference
Insights into transition state stabilization of the beta-1,4-glycosidase Cex by covalent intermediate accumulation in active site mutants., Notenboom V, Birsan C, Nitz M, Rose DR, Warren RA, Withers SG, Nat Struct Biol. 1998 Sep;5(9):812-8. PMID:9731776
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