Mannosidase

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (08:19, 11 July 2024) (edit) (undo)
 
(17 intermediate revisions not shown.)
Line 1: Line 1:
-
{{STRUCTURE_1fo2| PDB=1fo2 | SIZE=400| SCENE= |right| CAPTION=Human α-mannosidase class I complex with inhibitor deoxymannojirimycin, sulfate anc Ca+2 ion (green), [[1fo2]] }}
+
<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'>
 +
__TOC__
 +
== Function ==
-
'''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]].
+
'''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.
 +
* '''Endo-1,2-α-MAN''' is the Endo-acting glycoside hydrolase involved in N-glycan trimming located in the Golgi<ref>PMID:33154157</ref>
 +
See some details in [[Molecular Playground/ERMan1]]. See also [[Carbohydrate Metabolism]].
-
{{TOC limit|limit=2}}
+
== Disease ==
 +
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>.
 +
 
 +
== Structural highlights ==
 +
<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==
 +
[[Mannosidase 3D structures]]
-
Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
+
</StructureSection>
-
===α-MAN===
+
== References ==
-
 
+
<references/>
-
[[1hcu]] - αMAN – ''Trichoderma reesei''<br />
+
-
[[1o7d]] - αMAN – bovine<br />
+
-
[[2wvy]], [[2ww2]], [[4acy]], [[4acz]], [[4ad0]] - αMAN - ''Bacterioides thetaiotaomicron''
+
-
===α-MAN class I===
 
- 
-
[[1fmi]] - hαMAN I - human<br />
 
-
[[1fo2]] - hαMAN I + deoxymannojirimycin<br />
 
-
[[1fo3]] - hαMAN I+ kifunensine<br />
 
-
[[1dl2]] - αMAN I catalytic domain + mannose - yeast<br />
 
-
[[2ri8]] - PcαMAN I + glycerol – ''Penicillium citrinum''<br />
 
-
[[1kre]], [[1kkt]] - PcαMAN I + mannose<br />
 
-
[[2ri9]] - PcαMAN I + substrate analog<br />
 
-
[[1krf]] - PcαMAN I + kifunensine + mannose<br />
 
-
[[1x9d]] - hαMAN I residues 243-699 + polysaccharide analog<br />
 
-
[[1nxc]] - αMAN I + mannose – mouse<br />
 
-
[[1g6i]] - αMAN I + deoxymannojirimycin<br />
 
- 
-
===α-MAN class II===
 
- 
-
[[2wyh]] - SpαMAN II – ''Streptococcus pyrogenes''<br />
 
-
[[3bub]], [[1hty]] - DmαMAN II catalytic domain – ''Drosophila melanogaster''<br />
 
-
[[3bud]] - DmαMAN II catalytic domain (mutant) <br />
 
-
[[3bui]] - DmαMAN II catalytic domain (mutant) + Tris<br />
 
-
[[3bup]], [[3buq]], [[3czs]] - DmαMAN II catalytic domain (mutant) + mannose<br />
 
-
[[3bvt]], [[3bvu]], [[3bvv]], [[3bvw]], [[3bvx]] - DmαMAN II catalytic domain (mutant) + mannopyranoside<br />
 
-
[[1r33]], [[1r34]] - DmαMAN II catalytic domain + mannopyranoside<br />
 
-
[[3ddf]], [[3ddg]], [[2f18]], [[2f1a]], [[2f1b]] - DmαMAN II catalytic domain + pyrrolidin<br />
 
-
[[2alw]] - DmαMAN II catalytic domain + noeuromycin<br />
 
-
[[3cv5]] - DmαMAN II catalytic domain + polysaccharide<br />
 
-
[[3czn]] - DmαMAN II catalytic domain (mutant) + polysaccharide<br />
 
-
[[2wyi]] - SpαMAN II + swainsonine<br />
 
-
[[3blb]], [[1hww]] - DmαMAN II + swainsonine<br />
 
-
[[3ejp]], [[3ejq]], [[3ejr]], [[3ejs]], [[3ejt]], [[3eju]], [[2ow6]], [[2ow7]] - DmαMAN II catalytic domain + swainsonine analog<br />
 
-
[[3dx0]], [[3dx2]], [[2f7o]] - DmαMAN II catalytic domain + mannostatine<br />
 
-
[[3dx1]], [[3dx3]], [[3dx4]], [[2f7p]] - DmαMAN II catalytic domain + mannostatine analog<br />
 
-
[[3d4y]], [[3d4z]] - DmαMAN II catalytic domain + imidazole derivative<br />
 
-
[[3d50]], [[3d51]], [[3d52]] - DmαMAN II catalytic domain + inhibitor<br />
 
-
[[2fyv]], [[2f7q]], [[2f7r]] - DmαMAN II catalytic domain + amino-salacinol carboxylate analog<br />
 
-
[[1tqv]], [[1tqw]], [[1tqs]], [[1tqt]], [[1tqu]] - DmαMAN II catalytic domain (mutant) + seleno-salacinol<br />
 
-
[[1ps3]] - DmαMAN II catalytic domain + kifunensine<br />
 
-
[[1qwn]] - DmαMAN II catalytic domain + intermediate<br />
 
-
[[1hxk]] - DmαMAN II catalytic domain + deoxymannojirimycin<br />
 
-
[[1qwu]] - DmαMAN II catalytic domain (mutant) + guloside<br />
 
-
[[1qx1]] - DmαMAN II catalytic domain (mutant) + mannosyl
 
- 
-
===α-1,2-MAN===
 
- 
-
[[4ayo]] – CaαMAN - ''Caulobacter''<br />
 
-
[[4ayp]], [[4ayq]] – CaαMAN + mannose derivative<br />
 
-
[[4ayr]] – CaαMAN + noeuromycin<br />
 
- 
-
===β-MAN===
 
- 
-
[[2je8]] - BtβMAN residues 26-864 <br />
 
-
[[2wbk]] - BtβMAN residues 26-864 + mannopyranoside <br />
 
-
[[2vqt]], [[2vr4]], [[2vjx]], [[2vl4]], [[2vmf]], [[2vo5]], [[2vot]], [[2vqu]] - BtβMAN residues 26-864 + piperidine derivative<br />
 
-
[[1oh4]], [[1of4]] - TmβMAN catalytic domain + mannose – ''Thermotoga maritima''<br />
 
-
[[1of3]] - TmβMAN catalytic domain<br />
 
-
[[1uz4]] - CmβMAN + inhibitor – ''Cellvibrio mixtus''<br />
 
-
[[1uuq]] - CmβMAN<br />
 
-
[[2whk]] - βMAN – ''Bacillus subtilis''<br />
 
-
[[4jho]] - rβMAN – rice<br />
 
-
[[4jie]] - rβMAN + β-mannose<br />
 
- 
-
===Mannan endo-1,4-β-MAN===
 
- 
-
[[1gvy]], [[1odz]], [[1gw1]], [[2whm]] - PcβMAN (mutant) + mannose derivative – ''Pseudomonas cellulosa''<br />
 
-
[[1j9y]], [[1r7o]] - PcβMAN<br />
 
-
[[2c0h]] - βMAN (mutant) – blue mussel<br />
 
-
[[2whk]] - βMAN – ''Bacillus subtilis''<br />
 
-
[[1rh9]] – βMAN – ''Solanum lycopersicum''<br />
 
-
[[3pz9]], [[3pzg]] – TpβMAN – ''Thermotoga petrophila''<br />
 
-
[[3pzi]] – TpβMAN + glucose<br />
 
-
[[3pzm]], [[3pzn]] – TpβMAN + glycerol<br />
 
-
[[3pzo]], [[3pzq]] – TpβMAN + maltose
 
- 
- 
- 
-
 
- 
- 
- 
[[Category:Topic Page]]
[[Category:Topic Page]]

Current revision

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

Drag the structure with the mouse to rotate

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

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky

Retrieved from "http://52.214.119.220/wiki/index.php/Mannosidase"
Personal tools