alpha-Mannosidase

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

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:

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

↑ “PyMol”. Schrodinger. Retrieved 2011-09-14.
↑ 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.
↑ 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.
↑ Winchester, B. (1984). “Role of α-D-mannosidases in the biosynthesis and catabolism of glycoproteins”. Biochem. Soc. Trans. 12 (3): 522–524. PMID 6428944.
↑ 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.
↑ 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)

[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.

[pmid19520203-5] 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.

[pmid18651971-6] 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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