1g01

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spinqualitylabelsall models 1g01, resolution 1.9Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

ALKALINE CELLULASE K CATALYTIC DOMAIN

Overview

The crystal structure of the catalytic domain of alkaline cellulase K was, determined at 1.9 A resolution. Because of the most alkaliphilic nature, and it's highest activity at pH 9.5, it is used commercially in laundry, detergents. An analysis of the structural bases of the alkaliphilic, character of the enzyme suggested a mechanism similar to that previously, proposed for alkaline proteases, that is, an increase in the number of, Arg, His, and Gln residues, and a decrease in Asp and Lys residues. Some, ion pairs were formed by the gained Arg residues, which is similar to what, has been found in the alkaline proteases. Lys-Asp ion pairs are disfavored, and partly replaced with Arg-Asp ion pairs. The alkaline adaptation, appeared to be a remodeling of ion pairs so that the charge balance is, kept in the high pH range.

About this Structure

1G01 is a Single protein structure of sequence from Bacillus sp. with CD and ACY as ligands. Active as Cellulase, with EC number 3.2.1.4 Full crystallographic information is available from OCA.

Reference

Crystal structure of alkaline cellulase K: insight into the alkaline adaptation of an industrial enzyme., Shirai T, Ishida H, Noda J, Yamane T, Ozaki K, Hakamada Y, Ito S, J Mol Biol. 2001 Jul 27;310(5):1079-87. PMID:11501997

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