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β-Mannosidase

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(Redirected from EC 3.2.1.25)
MANBA
Identifiers
AliasesMANBA, MANB1, mannosidase beta
External IDsOMIM: 609489; MGI: 88175; HomoloGene: 4317; GeneCards: MANBA; OMA:MANBA - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
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

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

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

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  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000109323Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000028164Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ a b "Entrez Gene: mannosidase".
  6. ^ 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.
  7. ^ 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.
  8. ^ 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.
  9. ^ 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.
  10. ^ 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

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