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Mannosidase

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<StructureSection load='4jie' size='350' side='right' caption='Rice β-mannosidase complex with β-mannose, glycerol and hepes (PDB entry [[2pm4]])' scene=''>
<StructureSection load='4jie' size='350' side='right' caption='Rice β-mannosidase complex with β-mannose, glycerol and hepes (PDB entry [[2pm4]])' scene=''>
__TOC__
__TOC__
== Function ==
== Function ==
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'''Mannosidase''' (MAN) is an enzyme which hydrolyzes mannose. There are 2 kinds of MAN. '''α-MAN''' which hydrolyzes α-mannose and '''β-MAN'''. See some details in [[Molecular Playground/ERMan1]].
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'''Mannosidase''' (MAN) is an enzyme which hydrolyzes mannose. There are 2 kinds of MAN. '''α-MAN''' which hydrolyzes α-mannose<ref>PMID:12634058</ref> and '''β-MAN'''. See some details in [[Molecular Playground/ERMan1]].
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== Structural highlights ==
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The active site of β-MAN contains β-mannose<ref>PMID:24100330</ref>.
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</StructureSection>
==3D structures of mannosidase==
==3D structures of mannosidase==

Revision as of 10:03, 18 April 2016

Rice β-mannosidase complex with β-mannose, glycerol and hepes (PDB entry 2pm4)

Drag the structure with the mouse to rotate

3D structures of mannosidase

Updated on 18-April-2016

References

  1. ↑ Heikinheimo P, Helland R, Leiros HK, Leiros I, Karlsen S, Evjen G, Ravelli R, Schoehn G, Ruigrok R, Tollersrud OK, McSweeney S, Hough E. The structure of bovine lysosomal alpha-mannosidase suggests a novel mechanism for low-pH activation. J Mol Biol. 2003 Mar 28;327(3):631-44. PMID:12634058
  2. ↑ Tankrathok A, Iglesias-Fernandez J, Luang S, Robinson RC, Kimura A, Rovira C, Hrmova M, Ketudat Cairns JR. Structural analysis and insights into the glycon specificity of the rice GH1 Os7BGlu26 beta-D-mannosidase. Acta Crystallogr D Biol Crystallogr. 2013 Oct;69(Pt 10):2124-35. doi:, 10.1107/S0907444913020568. Epub 2013 Sep 20. PMID:24100330 doi:http://dx.doi.org/10.1107/S0907444913020568

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Michal Harel, Alexander Berchansky

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