Beta-mannosidase

From Wikipedia, the free encyclopedia
Jump to: navigation, search
For other uses of the term "MANBA", see Manba (disambiguation).
Mannosidase, beta A, lysosomal
Identifiers
Symbols MANBA ; MANB1
External IDs OMIM609489 MGI88175 HomoloGene4317 ChEMBL: 3903 GeneCards: MANBA Gene
EC number 3.2.1.25
Orthologs
Species Human Mouse
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:
103.55 – 103.68 Mb
Chr 3:
135.49 – 135.57 Mb
PubMed search [1] [2]
Beta-mannosidase
Identifiers
EC number 3.2.1.25
CAS number 9025-43-8
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / EGO

Beta-mannosidase (EC 3.2.1.25, mannanase, mannase, beta-D-mannosidase, beta-mannoside mannohydrolase, exo-beta-D-mannanase, lysosomal beta A mannosidase) is an enzyme with system name beta-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 beta-D-mannose residues in beta-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 beta-mannosidosis, a lysosomal storage disease that has a wide spectrum of neurological involvement.[1]

References[edit]

  1. ^ a b "Entrez Gene: mannosidase". 
  2. ^ 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. 
  3. ^ Adams, M., Richtmyer, N.K. and 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. and 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. and 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. and Sawai, K. (1964). "The enzymatic hydrolysis of Leucaena glauca galactomannan. Isolation of crystalline galactomannan depolymerase". J. Biol. Chem. 239: 990–992. PMID 14165949. 

Further reading[edit]