Biology:Β-Mannosidase

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Short description: Protein-coding gene in humans


A representation of the 3D structure of the protein myoglobin showing turquoise α-helices.
Generic protein structure example
β-Mannosidase
Identifiers
EC number3.2.1.25
CAS number9025-43-8
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO

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.[1][2][3][4][5][6] 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.[1]

References

  1. 1.0 1.1 "Entrez Gene: mannosidase". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4126. 
  2. "Molecular cloning and characterization of bovine beta-mannosidase". J. Biol. Chem. 270 (8): 3841–8. February 1995. doi:10.1074/jbc.270.8.3841. PMID 7876128. 
  3. 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. 
  4. 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. 
  5. 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. 
  6. 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

External links