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β-Mannosidase





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(Redirected from Mannanase)
  

For other uses of "MANBA", see Manba (disambiguation).

β-Mannosidase (EC 3.2.1.25}, mannanase, mannase, β-D-mannosidase, β-mannoside mannohydrolase, exo-β-D-mannanase, lysosomal β A mannosidase) is an enzyme with systematic name β-D-mannoside mannohydrolase, which is in humans encoded by the MANBA gene.[5][6][7][8][9][10] This enzyme catalyses the following chemical reaction

MANBA
Identifiers
AliasesMANBA, MANB1, mannosidase beta
External IDsOMIM: 609489; MGI: 88175; HomoloGene: 4317; GeneCards: MANBA; OMA:MANBA - orthologs
Orthologs
SpeciesHumanMouse
Entrez

4126

110173

Ensembl

ENSG00000109323

ENSMUSG00000028164

UniProt

O00462

Q8K2I4

RefSeq (mRNA)

NM_005908

NM_027288

RefSeq (protein)

NP_005899

NP_081564

Location (UCSC)Chr 4: 102.63 – 102.76 MbChr 3: 135.19 – 135.28 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse
β-Mannosidase
Identifiers
EC no.3.2.1.25
CAS no.9025-43-8
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins
Hydrolysis of terminal, non-reducing β-D-mannose residues in β-D-mannosides

This gene encodes a member of the glycosyl hydrolase 2 family. The encoded protein localizes to the lysosome where it is the final exoglycosidase in the pathway for N-linked glycoprotein oligosaccharide catabolism. Mutations in this gene are associated with β-mannosidosis, a lysosomal storage disease that has a wide spectrum of neurological involvement.[5]

References

edit
  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000109323 – Ensembl, May 2017
  • ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000028164 – Ensembl, May 2017
  • ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  • ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  • ^ a b "Entrez Gene: mannosidase".
  • ^ Chen H, Leipprandt JR, Traviss CE, Sopher BL, Jones MZ, Cavanagh KT, Friderici KH (February 1995). "Molecular cloning and characterization of bovine beta-mannosidase". J. Biol. Chem. 270 (8): 3841–8. doi:10.1074/jbc.270.8.3841. PMID 7876128.
  • ^ Adams, M.; Richtmyer, N.K. & Hudson, C.S. (1943). "Some enzymes present in highly purified invertase preparations; a contribution to the study of fructofuranosidases, galactosidases, glucosidases and mannosidases". J. Am. Chem. Soc. 65 (7): 1369–1380. doi:10.1021/ja01247a029.
  • ^ Bartholomew, B.A. & Perry, A.L. (1973). "The properties of synovial fluid β-mannosidase activity". Biochim. Biophys. Acta. 315 (1): 123–127. doi:10.1016/0005-2744(73)90136-8. PMID 4743897.
  • ^ Deuel, H.; Lewuenberger, R. & Huber, G. (1950). "Über den enzymatischen Abbau von Carubin, dem Galaktomannan aus Ceratonia siliqua L". Helv. Chim. Acta. 33 (4): 942–946. doi:10.1002/hlca.19500330424.
  • ^ Hylin, J.W. & Sawai, K. (1964). "The enzymatic hydrolysis of Leucaena glauca galactomannan. Isolation of crystalline galactomannan depolymerase". J. Biol. Chem. 239: 990–992. doi:10.1016/S0021-9258(18)91377-3. PMID 14165949.

    • Further reading

    edit
  • Kalsi G, Kuo PH, Aliev F, et al. (2010). "A systematic gene-based screen of chr4q22-q32 identifies association of a novel susceptibility gene, DKK2, with the quantitative trait of alcohol dependence symptom counts". Hum. Mol. Genet. 19 (12): 2497–506. doi:10.1093/hmg/ddq112. PMC 2876884. PMID 20332099.
  • Levade T, Graber D, Flurin V, et al. (1994). "Human β-mannosidase deficiency associated with peripheral neuropathy". Ann. Neurol. 35 (1): 116–9. doi:10.1002/ana.410350119. PMID 8285582. S2CID 71932852.
  • Hu H, Shioda T, Moriya C, et al. (1996). "Infectivities of human and other primate lentiviruses are activated by desialylation of the virion surface". J. Virol. 70 (11): 7462–70. doi:10.1128/jvi.70.11.7462-7470.1996. PMC 190813. PMID 8892864.
  • Yeh JC, Seals JR, Murphy CI, et al. (1993). "Site-specific N-glycosylation and oligosaccharide structures of recombinant HIV-1 gp120 derived from a baculovirus expression system". Biochemistry. 32 (41): 11087–99. doi:10.1021/bi00092a019. PMID 8218172.
  • Sabourdy F, Labauge P, Stensland HM, et al. (2009). "A MANBA mutation resulting in residual beta-mannosidase activity associated with severe leukoencephalopathy: a possible pseudodeficiency variant". BMC Med. Genet. 10: 84. doi:10.1186/1471-2350-10-84. PMC 2745377. PMID 19728872.
  • Hosgood HD, Zhang L, Shen M, et al. (2009). "Association between genetic variants in VEGF, ERCC3 and occupational benzene haematotoxicity". Occup Environ Med. 66 (12): 848–53. doi:10.1136/oem.2008.044024. PMC 2928224. PMID 19773279.
  • Alkhayat AH, Kraemer SA, Leipprandt JR, et al. (1998). "Human beta-mannosidase cDNA characterization and first identification of a mutation associated with human beta-mannosidosis". Hum. Mol. Genet. 7 (1): 75–83. doi:10.1093/hmg/7.1.75. PMID 9384606.
  • Kimura K, Wakamatsu A, Suzuki Y, et al. (2006). "Diversification of transcriptional modulation: large-scale identification and characterization of putative alternative promoters of human genes". Genome Res. 16 (1): 55–65. doi:10.1101/gr.4039406. PMC 1356129. PMID 16344560.
  • Papandreou MJ, Fenouillet E (1997). "Effect of various glycosidase treatments on the resistance of the HIV-1 envelope to degradation". FEBS Lett. 406 (1–2): 191–5. doi:10.1016/S0014-5793(97)00273-1. PMID 9109416. S2CID 17660.
  • Gao J, Arbman G, He L, et al. (2008). "MANBA polymorphism was related to increased risk of colorectal cancer in Swedish but not in Chinese populations". Acta Oncol. 47 (3): 372–8. doi:10.1080/02841860701644052. PMID 17899454. S2CID 45674826.
  • Robinson WE, Montefiori DC, Mitchell WM (1987). "Evidence that mannosyl residues are involved in human immunodeficiency virus type 1 (HIV-1) pathogenesis". AIDS Res. Hum. Retroviruses. 3 (3): 265–82. doi:10.1089/aid.1987.3.265. PMID 2829950.
  • Montefiori DC, Robinson WE, Mitchell WM (1988). "Role of protein N-glycosylation in pathogenesis of human immunodeficiency virus type 1". Proc. Natl. Acad. Sci. U.S.A. 85 (23): 9248–52. Bibcode:1988PNAS...85.9248M. doi:10.1073/pnas.85.23.9248. PMC 282716. PMID 3264072.
  • Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
  • Fenouillet E, Jones I, Powell B, et al. (1993). "Functional role of the glycan cluster of the human immunodeficiency virus type 1 transmembrane glycoprotein (gp41) ectodomain". J. Virol. 67 (1): 150–60. doi:10.1128/jvi.67.1.150-160.1993. PMC 237347. PMID 8093218.
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2002). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
  • Land A, Braakman I (2001). "Folding of the human immunodeficiency virus type 1 envelope glycoprotein in the endoplasmic reticulum". Biochimie. 83 (8): 783–90. doi:10.1016/S0300-9084(01)01314-1. hdl:1874/5091. PMID 11530211. S2CID 13576808.
  • Blough HA, Pauwels R, De Clercq E, et al. (1986). "Glycosylation inhibitors block the expression of LAV/HTLV-III (HIV) glycoproteins". Biochem. Biophys. Res. Commun. 141 (1): 33–8. doi:10.1016/S0006-291X(86)80330-8. PMID 3099781.
  • Hart ML, Saifuddin M, Spear GT (2003). "Glycosylation inhibitors and neuraminidase enhance human immunodeficiency virus type 1 binding and neutralization by mannose-binding lectin". J. Gen. Virol. 84 (Pt 2): 353–60. doi:10.1099/vir.0.18734-0. PMID 12560567.
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    Last edited on 23 June 2024, at 01:14  





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