alpha-Mannosidase

From Wikipedia, the free encyclopedia
Jump to: navigation, search
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 is an enzyme involved in the cleavage of the alpha form of mannose.

Contents

[edit] 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

[edit] 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.[3]

[edit] Pathology

A deficiency can lead to alpha-mannosidosis.[4]

[edit] References

  1. ^ "PyMol". Schrodinger. http://www.pymol.org/. Retrieved 9/14/2011. 
  2. ^ Suits, MDL; Yanping Zhu, Edward J. Taylor, Julia Walton, David L. Zechel, Harry J. Gilbert, Gideon J. Davies (3). "Structure and Kinetic Investigation of Streptococcus pyogenes Family GH38 α-Mannosidase". Plos One 5 (2). http://www.plosone.org/article/info%3Adoi%2F10.1371%2Fjournal.pone.0009006. Retrieved 9/14/2011. 
  3. ^ 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. 
  4. ^ Malm D, Nilssen Ø (2008). "Alpha-mannosidosis.". Orphanet J Rare Dis 3: 21. doi:10.1186/1750-1172-3-21. PMC 2515294. PMID 18651971. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2515294. 

[edit] External links

Stub icon This hydrolase article is a stub. You can help Wikipedia by expanding it.
Hydrolase: sugar hydrolases (EC 3.2)
3.2.1: Glycoside hydrolases
Other
3.2.2: Hydrolysing
N-Glycosyl compounds
Anabolism
Catabolism
Transport
M6P tagging

M: MET

mt, k, c/g/r/p/y/i, f/h/s/l/o/e, a/u, n, m

k, cgrp/y/i, f/h/s/l/o/e, au, n, m, epon

m(A16/C10),i(k, c/g/r/p/y/i, f/h/s/o/e, a/u, n, m)
Retrieved from "http://en.wikipedia.org/w/index.php?title=Alpha-Mannosidase&oldid=452784702"
Personal tools
Namespaces

Variants
Actions
Navigation
Interaction
Toolbox
Print/export