Α-Mannosidase

Cartoon depiction of the protein Streptococcus pyogenes family GH38 α-Mannosidase created using PyMol.[1][2]
α-Mannosidase
α-Mannosidase 1, tetramer, Saccharomyces cerevisiae
Identifiers
EC no.3.2.1.24
CAS no.9025-42-7
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

α-Mannosidase (EC 3.2.1.24, α-D-mannosidase, p-nitrophenyl-α-mannosidase, α-D-mannopyranosidase, 1,2-α-mannosidase, 1,2-α-D-mannosidase, exo-α-mannosidase) is an enzyme involved in the cleavage of the α form of mannose. Its systematic name is α-D-mannoside mannohydrolase.[3][4]

Isoenzymes

Humans express the following three α-mannosidase isoenzymes:

mannosidase, α, class 2B, member 1
Identifiers
SymbolMAN2B1
Alt. symbolsMANB
NCBI gene4125
HGNC6826
OMIM609458
RefSeqNM_000528
UniProtO00754
Other data
EC number3.2.1.24
LocusChr. 19 cen-q13.1
Search for
StructuresSwiss-model
DomainsInterPro
mannosidase, α, class 2B, member 2
Identifiers
SymbolMAN2B2
Alt. symbolsKIAA0935
NCBI gene23324
HGNC29623
RefSeqNM_015274
UniProtQ9Y2E5
Other data
EC number3.2.1.24
LocusChr. 4 p16.2
Search for
StructuresSwiss-model
DomainsInterPro
mannosidase, α, class 2C, member 1
Identifiers
SymbolMAN2C1
Alt. symbolsMANA1, MANA
NCBI gene4123
HGNC6827
OMIM154580
RefSeqNM_006715
UniProtQ9NTJ4
Other data
EC number3.2.1.24
LocusChr. 15 q11-qter
Search for
StructuresSwiss-model
DomainsInterPro

Applications

It can be utilized in experiments that determine the effects of the presence or absence of mannose on specific molecules, such as recombinant proteins that are used in vaccine development.[5]

Pathology

A deficiency can lead to α-mannosidosis.[6]

References

  1. ^ "PyMol". Schrodinger. Retrieved 2011-09-14.
  2. ^ Suits, MDL; Yanping Zhu; Edward J. Taylor; Julia Walton; David L. Zechel; Harry J. Gilbert; Gideon J. Davies (3 February 2010). "Structure and Kinetic Investigation of Streptococcus pyogenes Family GH38 α-Mannosidase". PLOS ONE. 5 (2): e9006. Bibcode:2010PLoSO...5.9006S. doi:10.1371/journal.pone.0009006. PMC 2815779. PMID 20140249.
  3. ^ Li, Y.-T. (1966). "Presence of α-D-mannosidic linkage in glycoproteins. Liberation of D-mannose from various glycoproteins by α-mannosidase isolated from jack bean meal". J. Biol. Chem. 241 (4): 1010–1012. doi:10.1016/S0021-9258(18)96865-1. PMID 5905120.
  4. ^ Winchester, B. (1984). "Role of α-D-mannosidases in the biosynthesis and catabolism of glycoproteins". Biochem. Soc. Trans. 12 (3): 522–524. doi:10.1042/bst0120522. PMID 6428944.
  5. ^ Vlahopoulos S, Gritzapis AD, Perez SA, Cacoullos N, Papamichail M, Baxevanis CN (2009). "Mannose addition by yeast Pichia Pastoris on recombinant HER-2 protein inhibits recognition by the monoclonal antibody herceptin". Vaccine. 27 (34): 4704–8. doi:10.1016/j.vaccine.2009.05.063. PMID 19520203.
  6. ^ Malm D, Nilssen Ø (2008). "Alpha-mannosidosis". Orphanet J Rare Dis. 3: 21. doi:10.1186/1750-1172-3-21. PMC 2515294. PMID 18651971.


This EC 3.2 enzyme-related article is a stub. You can help Wikipedia by expanding it.