(Redirected from
Alpha-Mannosidase)
| α-Mannosidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 α-Mannosidase 1, tetramer, Saccharomyces cerevisiae | |||||||||
| Identifiers | |||||||||
| EC no. | 3.2.1.24 | ||||||||
| CAS no. | 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 / QuickGO | ||||||||
| |||||||||
α-Mannosidase ( EC 3.2.1.24, α-D-mannosidase, p-nitrophenyl-α-mannosidase, α-D-mannopyranosidase, 1,2-α-mannosidase, 1,2-α-D-mannosidase, exo-α-mannosidase) is an enzyme involved in the cleavage of the α form of mannose. Its systematic name is α-D-mannoside mannohydrolase. [3] [4]
Isoenzymes
Humans express the following three α-mannosidase isoenzymes:
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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 α-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): e9006. Bibcode: 2010PLoSO...5.9006S. doi: 10.1371/journal.pone.0009006. PMC 2815779. PMID 20140249.
- ^ 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. doi: 10.1016/S0021-9258(18)96865-1. PMID 5905120.
- ^ Winchester, B. (1984). "Role of α-D-mannosidases in the biosynthesis and catabolism of glycoproteins". Biochem. Soc. Trans. 12 (3): 522–524. doi: 10.1042/bst0120522. 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 U.S. National Library of Medicine Medical Subject Headings (MeSH)
(Redirected from
Alpha-Mannosidase)
| α-Mannosidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
|
α-Mannosidase 1, tetramer, Saccharomyces cerevisiae | |||||||||
| Identifiers | |||||||||
| EC no. | 3.2.1.24 | ||||||||
| CAS no. | 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 / QuickGO | ||||||||
| |||||||||
α-Mannosidase ( EC 3.2.1.24, α-D-mannosidase, p-nitrophenyl-α-mannosidase, α-D-mannopyranosidase, 1,2-α-mannosidase, 1,2-α-D-mannosidase, exo-α-mannosidase) is an enzyme involved in the cleavage of the α form of mannose. Its systematic name is α-D-mannoside mannohydrolase. [3] [4]
Isoenzymes
Humans express the following three α-mannosidase isoenzymes:
|
|
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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 α-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): e9006. Bibcode: 2010PLoSO...5.9006S. doi: 10.1371/journal.pone.0009006. PMC 2815779. PMID 20140249.
- ^ 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. doi: 10.1016/S0021-9258(18)96865-1. PMID 5905120.
- ^ Winchester, B. (1984). "Role of α-D-mannosidases in the biosynthesis and catabolism of glycoproteins". Biochem. Soc. Trans. 12 (3): 522–524. doi: 10.1042/bst0120522. 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 U.S. National Library of Medicine Medical Subject Headings (MeSH)