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

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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

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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

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

References

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  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.
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