Mannosidase
From Proteopedia
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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 == | ||
| - | '''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]]. | + | '''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]]. |
| + | == Structural highlights == | ||
| + | The active site of β-MAN contains β-mannose<ref>PMID:24100330</ref>. | ||
| + | </StructureSection> | ||
==3D structures of mannosidase== | ==3D structures of mannosidase== | ||
Revision as of 10:03, 18 April 2016
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3D structures of mannosidase
Updated on 18-April-2016
References
- ↑ 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
- ↑ 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
