alpha-Mannosidase

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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

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 system name is alpha-D-mannoside mannohydrolase.[3][4]

Isozymes[edit]

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[edit]

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[edit]

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

References[edit]

  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[edit]