alpha-Mannosidase

Cartoon depiction of the protein Streptococcus pyogenes family GH38 α-Mannosidase created using PyMol.^[1][2]

alpha-mannosidase
Identifiers
EC number	3.2.1.24
CAS number	9025-42-7
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
Search PMC articles PubMed articles NCBI proteins

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

Isozymes

Humans express the following three alpha-mannosidase isozymes:

mannosidase, alpha, class 2B, member 1 Identifiers Symbol MAN2B1 Alt. symbols MANB Entrez 4125 HUGO 6826 OMIM 609458 RefSeq NM_000528 UniProt O00754 Other data EC number 3.2.1.24 Locus Chr. 19 cen-q13.1

mannosidase, alpha, class 2B, member 2 Identifiers Symbol MAN2B2 Alt. symbols KIAA0935 Entrez 23324 HUGO 29623 RefSeq NM_015274 UniProt Q9Y2E5 Other data EC number 3.2.1.24 Locus Chr. 4 p16.2

mannosidase, alpha, class 2C, member 1 Identifiers Symbol MAN2C1 Alt. symbols MANA1, MANA Entrez 4123 HUGO 6827 OMIM 154580 RefSeq NM_006715 UniProt Q9NTJ4 Other data EC number 3.2.1.24 Locus Chr. 15 q11-qter

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 alpha-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). doi:10.1371/journal.pone.0009006. Retrieved 2011-09-14.
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. 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. 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.

External links

• GeneReviews/NCBI/NIH/UW entry on Alpha-Mannosidosis
• OMIM entries on Alpha-Mannosidosis
• alpha-Mannosidase at the US National Library of Medicine Medical Subject Headings (MeSH)