3axh

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[[Image:3axh.jpg|left|200px]]
 
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{{STRUCTURE_3axh| PDB=3axh | SCENE= }}
{{STRUCTURE_3axh| PDB=3axh | SCENE= }}
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===Crystal structure of isomaltase in complex with isomaltose===
===Crystal structure of isomaltase in complex with isomaltose===
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{{ABSTRACT_PUBMED_21925939}}
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==Function==
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[[http://www.uniprot.org/uniprot/MALX3_YEAST MALX3_YEAST]] Major isomaltase (alpha-1,6-glucosidase) required for isomaltose utilization. Preferentially hydrolyzes isomaltose, palatinose, and methyl-alpha-glucoside, with little activity towards isomaltotriose or longer oligosaccharides. Does not hydrolyze maltose.<ref>PMID:15291818</ref> <ref>PMID:20562106</ref>
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(as it appears on PubMed at http://www.pubmed.gov), where 21925939 is the PubMed ID number.
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{{ABSTRACT_PUBMED_21925939}}
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==About this Structure==
==About this Structure==
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==Reference==
==Reference==
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<ref group="xtra">PMID:021925939</ref><references group="xtra"/>
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<ref group="xtra">PMID:021925939</ref><references group="xtra"/><references/>
[[Category: Oligo-1,6-glucosidase]]
[[Category: Oligo-1,6-glucosidase]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]

Revision as of 08:38, 19 June 2013

Template:STRUCTURE 3axh

Contents

Crystal structure of isomaltase in complex with isomaltose

Template:ABSTRACT PUBMED 21925939

Function

[MALX3_YEAST] Major isomaltase (alpha-1,6-glucosidase) required for isomaltose utilization. Preferentially hydrolyzes isomaltose, palatinose, and methyl-alpha-glucoside, with little activity towards isomaltotriose or longer oligosaccharides. Does not hydrolyze maltose.[1] [2]

About this Structure

3axh is a 1 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

  • Yamamoto K, Miyake H, Kusunoki M, Osaki S. Steric hindrance by 2 amino acid residues determines the substrate specificity of isomaltase from Saccharomyces cerevisiae. J Biosci Bioeng. 2011 Sep 16. PMID:21925939 doi:10.1016/j.jbiosc.2011.08.016
  1. ↑ Yamamoto K, Nakayama A, Yamamoto Y, Tabata S. Val216 decides the substrate specificity of alpha-glucosidase in Saccharomyces cerevisiae. Eur J Biochem. 2004 Aug;271(16):3414-20. PMID:15291818 doi:10.1111/j.1432-1033.2004.04276.x
  2. ↑ Teste MA, Francois JM, Parrou JL. Characterization of a new multigene family encoding isomaltases in the yeast Saccharomyces cerevisiae, the IMA family. J Biol Chem. 2010 Aug 27;285(35):26815-24. doi: 10.1074/jbc.M110.145946. Epub, 2010 Jun 18. PMID:20562106 doi:10.1074/jbc.M110.145946

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