Alpha-Mannosidase

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

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]

Contents

  • Isozymes 1
  • Applications 2
  • Pathology 3
  • References 4
  • External links 5

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).  
  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.  
  4. ^ Winchester, B. (1984). "Role of α-D-mannosidases in the biosynthesis and catabolism of glycoproteins". Biochem. Soc. Trans. 12 (3): 522–524.  
  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.  
  6. ^ Malm D, Nilssen Ø (2008). "Alpha-mannosidosis.". Orphanet J Rare Dis 3: 21.  

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)