Mannosidase

From Proteopedia

Revision as of 07:54, 10 July 2017

spinqualitylabelsall models Rice β-mannosidase complex with β-mannose, glycerol and HEPES (PDB entry 4jie) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Contents 1 Function 2 Disease 3 Structural highlights Function Mannosidase (MAN) is an enzyme which hydrolyzes mannose. There are 2 kinds of MAN. α-MAN which hydrolyzes α-mannose[1] and β-MAN which hydrolyzes β-1,4-linked manno-oligosaccharides[2]. 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. Disease α-mannosidosis is manifested by accumulation of mannose-containing oligosaccharides leading to mental retardation, hearing impairment, skeletal changes and immunodeficiency[3]. β-MAN deficiency called β-mannosidosis is a disorder of oligosaccharide metabolism[4]. Structural highlights [5]. Water molecules shown as red spheres.

3D structures of mannosidase

Updated on 10-July-2017 {{#tree:id=OrganizedByTopic|openlevels=0|

• α-MAN

• • 1hcu - αMAN – Trichoderma reesei
    
  • 1o7d - αMAN – bovine
    
  • 2wvy, 2ww2, 4acy, 4acz, 4ad0 - αMAN - Bacterioides thetaiotaomicron

• α-MAN class I

• • 1fmi - hαMAN I - human
    
  • 1fo2 - hαMAN I + deoxymannojirimycin
    
  • 1fo3 - hαMAN I+ kifunensine
    
  • 5jm0 - yαMAN I – yeast
    
  • 1dl2 - yαMAN I catalytic domain + mannose - yeast
    
  • 2ri8 - PcαMAN I + glycerol – Penicillium citrinum
    
  • 1kre, 1kkt - PcαMAN I + mannose
    
  • 2ri9 - PcαMAN I + substrate analog
    
  • 1krf - PcαMAN I + kifunensine + mannose
    
  • 1x9d - hαMAN I residues 243-699 + polysaccharide analog
    
  • 1nxc - αMAN I + mannose – mouse
    
  • 1g6i - αMAN I + deoxymannojirimycin
    

• α-MAN class II

• • 2wyh - SpαMAN II – Streptococcus pyrogenes
    
  • 3bub, 1hty - DmαMAN II catalytic domain – Drosophila melanogaster
    
  • 3bud - DmαMAN II catalytic domain (mutant)
    
  • 3bui - DmαMAN II catalytic domain (mutant) + Tris
    
  • 3bup, 3buq, 3czs - DmαMAN II catalytic domain (mutant) + mannose
    
  • 3bvt, 3bvu, 3bvv, 3bvw, 3bvx - DmαMAN II catalytic domain (mutant) + mannopyranoside
    
  • 1r33, 1r34 - DmαMAN II catalytic domain + mannopyranoside
    
  • 3ddf, 3ddg, 2f18, 2f1a, 2f1b - DmαMAN II catalytic domain + pyrrolidin
    
  • 2alw - DmαMAN II catalytic domain + noeuromycin
    
  • 3cv5 - DmαMAN II catalytic domain + polysaccharide
    
  • 3czn - DmαMAN II catalytic domain (mutant) + polysaccharide
    
  • 2wyi - SpαMAN II + swainsonine
    
  • 3blb, 1hww - DmαMAN II + swainsonine
    
  • 3ejp, 3ejq, 3ejr, 3ejs, 3ejt, 3eju, 2ow6, 2ow7 - DmαMAN II catalytic domain + swainsonine analog
    
  • 3dx0, 3dx2, 2f7o - DmαMAN II catalytic domain + mannostatine
    
  • 3dx1, 3dx3, 3dx4, 2f7p - DmαMAN II catalytic domain + mannostatine analog
    
  • 3d4y, 3d4z - DmαMAN II catalytic domain + imidazole derivative
    
  • 3d50, 3d51, 3d52 - DmαMAN II catalytic domain + inhibitor
    
  • 2fyv, 2f7q, 2f7r - DmαMAN II catalytic domain + amino-salacinol carboxylate analog
    
  • 1tqv, 1tqw, 1tqs, 1tqt, 1tqu - DmαMAN II catalytic domain (mutant) + seleno-salacinol
    
  • 1ps3 - DmαMAN II catalytic domain + kifunensine
    
  • 1qwn - DmαMAN II catalytic domain + intermediate
    
  • 1hxk - DmαMAN II catalytic domain + deoxymannojirimycin
    
  • 1qwu - DmαMAN II catalytic domain (mutant) + guloside
    
  • 1qx1 - DmαMAN II catalytic domain (mutant) + mannosyl

• α-1,2-MAN

• • 4ayo – CaαMAN - Caulobacter
    
  • 4ayp, 4ayq – CaαMAN + mannose derivative
    
  • 4ayr – CaαMAN + noeuromycin
    

• β-MAN

• • 2je8 - BtβMAN residues 26-864
    
  • 2wbk - BtβMAN residues 26-864 + mannopyranoside
    
  • 2vqt, 2vr4, 2vjx, 2vl4, 2vmf, 2vo5, 2vot, 2vqu - BtβMAN residues 26-864 + piperidine derivative
    
  • 1oh4, 1of4 - TmβMAN catalytic domain + mannose – Thermotoga maritima
    
  • 1of3 - TmβMAN catalytic domain
    
  • 1uz4 - CmβMAN + inhibitor – Cellvibrio mixtus
    
  • 1uuq - CmβMAN
    
  • 2whk - βMAN – Bacillus subtilis
    
  • 4jho - rβMAN – rice
    
  • 4jie - rβMAN + β-mannose
    
  • 4cvu, 4uoj – βMAN - Trichoderma harzianum
    
  • 5n6u - βMAN + β-mannose – Dictyoglomus thermophilum
    

• Mannan endo-1,4-β-MAN

• • 1gvy, 1odz, 1gw1, 2whm - PcβMAN (mutant) + mannose derivative – Pseudomonas cellulosa
    
  • 1j9y, 1r7o - PcβMAN
    
  • 2c0h - βMAN (mutant) – blue mussel
    
  • 2whk, 4yn5 - βMAN – Bacillus subtilis
    
  • 1rh9 – βMAN – Solanum lycopersicum
    
  • 3pz9, 3pzg – TpβMAN – Thermotoga petrophila
    
  • 3pzi – TpβMAN + glucose
    
  • 3pzm, 3pzn – TpβMAN + glycerol
    
  • 3pzo, 3pzq – TpβMAN + maltose

• Exo-β-1,4-MAN

• • 4lyp - RmβMAN – Rhizomucor miehei
    
  • 4lyq, 4lyr - RmβMAN (mutant)
    
  • 4nrr - RmβMAN (mutant) + mannosyl-fructose
    
  • 4nrs - RmβMAN (mutant) + mannobiose
    

• Exo-α-1,6-MAN

• • 5m7i - CpαMAN (mutant) + mannobiose – Clostridium perfringenes
    
  • 5m7i - CpαMAN (mutant) + mannotriose
    

• β-MAN/β-glucosidase

• • [[4re2, 4re3, 4re4 - rβMAN/βGLU – rice
    

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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