1g01

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{{STRUCTURE_1g01| PDB=1g01 | SCENE= }}
{{STRUCTURE_1g01| PDB=1g01 | SCENE= }}
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'''ALKALINE CELLULASE K CATALYTIC DOMAIN'''
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===ALKALINE CELLULASE K CATALYTIC DOMAIN===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 11501997 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11501997}}
==About this Structure==
==About this Structure==
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[[Category: Alpha/beta barrel]]
[[Category: Alpha/beta barrel]]
[[Category: Tim barrel]]
[[Category: Tim barrel]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 04:11:50 2008''

Revision as of 01:11, 1 July 2008

Image:1g01.png

Template:STRUCTURE 1g01

ALKALINE CELLULASE K CATALYTIC DOMAIN

Template:ABSTRACT PUBMED 11501997

About this Structure

1G01 is a Single protein structure of sequence from Bacillus sp.. 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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