3mil

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{{STRUCTURE_3mil| PDB=3mil | SCENE= }}
{{STRUCTURE_3mil| PDB=3mil | SCENE= }}
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===Crystal structure of isoamyl acetate-hydrolyzing esterase from Saccharomyces cerevisiae===
===Crystal structure of isoamyl acetate-hydrolyzing esterase from Saccharomyces cerevisiae===
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==Function==
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[[http://www.uniprot.org/uniprot/IAH1_YEAST IAH1_YEAST]] Plays a crucial role in the hydrolysis of isoamyl acetate in sake mash.
==About this Structure==
==About this Structure==
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3MIL is a 2 chains structure with sequences from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MIL OCA].
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[[3mil]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MIL OCA].
==Reference==
==Reference==
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<ref group="xtra">PMID:21069734</ref><references group="xtra"/>
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<ref group="xtra">PMID:021069734</ref><references group="xtra"/><references/>
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Ge, H.]]
[[Category: Ge, H.]]
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[[Category: Hydrolase]]
[[Category: Hydrolase]]
[[Category: Sgnh-hydrolase]]
[[Category: Sgnh-hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Nov 24 14:15:31 2010''
 

Revision as of 21:08, 17 April 2013

Template:STRUCTURE 3mil

Contents

Crystal structure of isoamyl acetate-hydrolyzing esterase from Saccharomyces cerevisiae

Function

[IAH1_YEAST] Plays a crucial role in the hydrolysis of isoamyl acetate in sake mash.

About this Structure

3mil is a 2 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

  • Ma J, Lu Q, Yuan Y, Ge H, Li K, Zhao W, Gao Y, Niu L, Teng M. Crystal structure of isoamyl acetate-hydrolyzing esterase from Saccharomyces cerevisiae reveals a novel active site architecture and the basis of substrate specificity. Proteins. 2010 Sep 9. PMID:21069734 doi:10.1002/prot.22865

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