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Mannosidase

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{{STRUCTURE_1fo2| PDB=1fo2 | SIZE=300| SCENE= |right| CAPTION=Human α-mannosidase class I complex with inhibitor deoxymannojirimycine, [[1fo2]] }}
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<StructureSection load='4jie' size='350' side='right' caption='Rice β-mannosidase complex with β-mannose, glycerol and HEPES (PDB entry [[4jie]])' scene='45/458458/Cv/1'>
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__TOC__
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== Function ==
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'''Mannosidase''' (MAN) is an enzyme which hydrolyzes mannose. There are 2 kinds of MAN. αMAN which hydrolyzes α-mannose and βMAN.
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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''' which hydrolyzes β-1,4-linked manno-oligosaccharides<ref>PMID:10553664</ref>. α-MAN isozymes are classified as class I and II. '''Mannan endo-1,4-β-MAN''' hydrolyzes 1-4-β-D-mannosidic linkages in mannans, galactomannans and glucomannans. See some details in [[Molecular Playground/ERMan1]]. See also [[Carbohydrate Metabolism]].
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{{TOC limit|limit=2}}
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== Disease ==
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α-mannosidosis is manifested by accumulation of mannose-containing oligosaccharides leading to mental retardation, hearing impairment, skeletal changes and immunodeficiency<ref>PMID:9915946</ref>. β-MAN deficiency called β-mannosidosis is a disorder of oligosaccharide metabolism<ref>PMID:12890191</ref>.
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==3D structures of mannosidase==
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== Structural highlights ==
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<scene name='45/458458/Cv/5'>The active site of β-MAN contains β-mannose</scene><ref>PMID:24100330</ref>. Water molecules shown as red spheres.
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==3D structures of mannosidase==
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[[Mannosidase 3D structures]]
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</StructureSection>
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== References ==
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<references/>
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[[Category:Topic Page]]
[[Category:Topic Page]]

Current revision

Rice β-mannosidase complex with β-mannose, glycerol and HEPES (PDB entry 4jie)

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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. ↑ Ademark P, Lundqvist J, Hagglund P, Tenkanen M, Torto N, Tjerneld F, Stalbrand H. Hydrolytic properties of a beta-mannosidase purified from Aspergillus niger. J Biotechnol. 1999 Oct 8;75(2-3):281-9. PMID:10553664
  3. ↑ Berg T, Riise HM, Hansen GM, Malm D, Tranebjaerg L, Tollersrud OK, Nilssen O. Spectrum of mutations in alpha-mannosidosis. Am J Hum Genet. 1999 Jan;64(1):77-88. PMID:9915946 doi:http://dx.doi.org/S0002-9297(07)61660-7
  4. ↑ Uchino Y, Fukushige T, Yotsumoto S, Hashiguchi T, Taguchi H, Suzuki N, Konohana I, Kanzaki T. Morphological and biochemical studies of human beta-mannosidosis: identification of a novel beta-mannosidase gene mutation. Br J Dermatol. 2003 Jul;149(1):23-9. PMID:12890191
  5. ↑ 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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