2iuo

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m (Protected "2iuo" [edit=sysop:move=sysop])
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[[Image:2iuo.png|left|200px]]
 
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{{STRUCTURE_2iuo| PDB=2iuo | SCENE= }}
{{STRUCTURE_2iuo| PDB=2iuo | SCENE= }}
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===Site Directed Mutagenesis of Key Residues Involved in the Catalytic Mechnism of Cyanase===
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{{ABSTRACT_PUBMED_10801492}}
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===SITE DIRECTED MUTAGENESIS OF KEY RESIDUES INVOLVED IN THE CATALYTIC MECHANISM OF CYANASE===
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==Function==
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[[http://www.uniprot.org/uniprot/CYNS_ECOLI CYNS_ECOLI]] Catalyzes the reaction of cyanate with bicarbonate to produce ammonia and carbon dioxide.
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==About this Structure==
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[[2iuo]] is a 10 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IUO OCA].
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==About this Structure==
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==Reference==
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[[2iuo]] is a 10 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IUO OCA].
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<ref group="xtra">PMID:010801492</ref><references group="xtra"/><references/>
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[[Category: Bacillus coli migula 1895]]
[[Category: Cyanase]]
[[Category: Cyanase]]
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[[Category: Escherichia coli]]
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[[Category: Anderson, M P.]]
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[[Category: Anderson, P M.]]
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[[Category: Guilloton, M.]]
[[Category: Guilloton, M.]]
[[Category: Joachimiak, A.]]
[[Category: Joachimiak, A.]]

Revision as of 08:49, 5 February 2014

Template:STRUCTURE 2iuo

Contents

Site Directed Mutagenesis of Key Residues Involved in the Catalytic Mechnism of Cyanase

Template:ABSTRACT PUBMED 10801492

Function

[CYNS_ECOLI] Catalyzes the reaction of cyanate with bicarbonate to produce ammonia and carbon dioxide.

About this Structure

2iuo is a 10 chain structure with sequence from "bacillus_coli"_migula_1895 "bacillus coli" migula 1895. Full crystallographic information is available from OCA.

Reference

  • Walsh MA, Otwinowski Z, Perrakis A, Anderson PM, Joachimiak A. Structure of cyanase reveals that a novel dimeric and decameric arrangement of subunits is required for formation of the enzyme active site. Structure. 2000 May 15;8(5):505-14. PMID:10801492

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