Mannosidase

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{{STRUCTURE_1fo2| PDB=1fo2 | SIZE=400| SCENE= |right| CAPTION=Human α-mannosidase class I complex with inhibitor deoxymannojirimycin, sulfate anc Ca+2 ion, [[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. 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''' which hydrolyzes β-1,4-linked manno-oligosaccharides<ref>PMID:10553664</ref>. α-MAN isozymes are classified as class I and II.
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* '''Mannan endo-1,4-β-MAN''' hydrolyzes 1-4-β-D-mannosidic linkages in mannans, galactomannans and glucomannans.
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* '''Endo-1,2-α-MAN''' is the Endo-acting glycoside hydrolase involved in N-glycan trimming located in the Golgi<ref>PMID:33154157</ref>
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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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== 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.
==3D structures of mannosidase==
==3D structures of mannosidase==
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[[Mannosidase 3D structures]]
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''Updated December 2011''
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</StructureSection>
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===α-MAN===
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== References ==
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<references/>
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[[1hcu]] - αMAN – ''Trichoderma reesei''<br />
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[[1o7d]] - αMAN – bovine<br />
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[[2wvy]], [[2ww2]] - αMAN - ''Bacterioides thetaiotaomicron''
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===α-MAN class I===
 
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[[1fmi]] - hαMAN I - human<br />
 
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[[1fo2]] - hαMAN I + deoxymannojirimycin<br />
 
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[[1fo3]] - hαMAN I+ kifunensine<br />
 
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[[1dl2]] - αMAN I catalytic domain + mannose - yeast<br />
 
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[[2ri8]] - PcαMAN I + glycerol – ''Penicillium citrinum''<br />
 
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[[1kre]], [[1kkt]] - PcαMAN I + mannose<br />
 
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[[2ri9]] - PcαMAN I + substrate analog<br />
 
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[[1krf]] - PcαMAN I + kifunensine + mannose<br />
 
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[[1x9d]] - hαMAN I residues 243-699 + polysaccharide analog<br />
 
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[[1nxc]] - αMAN I + mannose – mouse<br />
 
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[[1g6i]] - αMAN I + deoxymannojirimycin<br />
 
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===α-MAN class II===
 
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[[2wyh]] - SpαMAN II – ''Streptococcus pyrogenes''<br />
 
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[[3bub]], [[1hty]] - DmαMAN II catalytic domain – ''Drosophila melanogaster''<br />
 
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[[3bud]] - DmαMAN II catalytic domain (mutant) <br />
 
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[[3bui]] - DmαMAN II catalytic domain (mutant) + Tris<br />
 
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[[3bup]], [[3buq]], [[3czs]] - DmαMAN II catalytic domain (mutant) + mannose<br />
 
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[[3bvt]], [[3bvu]], [[3bvv]], [[3bvw]], [[3bvx]] - DmαMAN II catalytic domain (mutant) + mannopyranoside<br />
 
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[[1r33]], [[1r34]] - DmαMAN II catalytic domain + mannopyranoside<br />
 
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[[3ddf]], [[3ddg]], [[2f18]], [[2f1a]], [[2f1b]] - DmαMAN II catalytic domain + pyrrolidin<br />
 
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[[2alw]] - DmαMAN II catalytic domain + noeuromycin<br />
 
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[[3cv5]] - DmαMAN II catalytic domain + polysaccharide<br />
 
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[[3czn]] - DmαMAN II catalytic domain (mutant) + polysaccharide<br />
 
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[[2wyi]] - SpαMAN II + swainsonine<br />
 
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[[3blb]], [[1hww]] - DmαMAN II + swainsonine<br />
 
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[[3ejp]], [[3ejq]], [[3ejr]], [[3ejs]], [[3ejt]], [[3eju]], [[2ow6]], [[2ow7]] - DmαMAN II catalytic domain + swainsonine analog<br />
 
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[[3dx0]], [[3dx2]], [[2f7o]] - DmαMAN II catalytic domain + mannostatine<br />
 
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[[3dx1]], [[3dx3]], [[3dx4]], [[2f7p]] - DmαMAN II catalytic domain + mannostatine analog<br />
 
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[[3d4y]], [[3d4z]] - DmαMAN II catalytic domain + imidazole derivative<br />
 
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[[3d50]], [[3d51]], [[3d52]] - DmαMAN II catalytic domain + inhibitor<br />
 
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[[2fyv]], [[2f7q]], [[2f7r]] - DmαMAN II catalytic domain + amino-salacinol carboxylate analog<br />
 
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[[1tqv]], [[1tqw]], [[1tqs]], [[1tqt]], [[1tqu]] - DmαMAN II catalytic domain (mutant) + seleno-salacinol<br />
 
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[[1ps3]] - DmαMAN II catalytic domain + kifunensine<br />
 
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[[1qwn]] - DmαMAN II catalytic domain + intermediate<br />
 
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[[1hxk]] - DmαMAN II catalytic domain + deoxymannojirimycin<br />
 
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[[1qwu]] - DmαMAN II catalytic domain (mutant) + guloside<br />
 
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[[1qx1]] - DmαMAN II catalytic domain (mutant) + mannosyl
 
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===β-MAN===
 
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[[2je8]] - BtβMAN residues 26-864 <br />
 
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[[2wbk]] - BtβMAN residues 26-864 + mannopyranoside <br />
 
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[[2vqt]], [[2vr4]], [[2vjx]], [[2vl4]], [[2vmf]], [[2vo5]], [[2vot]], [[2vqu]] - BtβMAN residues 26-864 + piperidine derivative<br />
 
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[[1oh4]], [[1of4]] - TmβMAN catalytic domain + mannose – ''Thermotoga maritima''<br />
 
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[[1of3]] - TmβMAN catalytic domain<br />
 
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[[1gvy]] - βMAN (mutant) + mannotrioside – ''Pseudomonas cellulose''<br />
 
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[[1uz4]] - CmβMAN + inhibitor – ''Cellvibrio mixtus''<br />
 
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[[1uuq]] - CmβMAN<br />
 
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[[2c0h]] - βMAN (mutant) – blue mussel<br />
 
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[[2whk]] - βMAN – ''Bacillus subtilis''
 
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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. ↑ Sobala LF, Fernandes PZ, Hakki Z, Thompson AJ, Howe JD, Hill M, Zitzmann N, Davies S, Stamataki Z, Butters TD, Alonzi DS, Williams SJ, Davies GJ. Structure of human endo-alpha-1,2-mannosidase (MANEA), an antiviral host-glycosylation target. Proc Natl Acad Sci U S A. 2020 Nov 5. pii: 2013620117. doi:, 10.1073/pnas.2013620117. PMID:33154157 doi:http://dx.doi.org/10.1073/pnas.2013620117
  4. ↑ 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
  5. ↑ 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
  6. ↑ 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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