|Gene:||ALG1||Accession Number: G-5561 (MetaCyc)|
Synonyms: GDP-mannose: dolichyl diphosphate chitobiose mannosyl transferase
Species: Saccharomyces cerevisiae
Residues 8-24 of the protein contain hydrophobic amino acids, and this region is predicted to form a signal sequence and membrane spanning domain [Albright90]. This region also contains a 13-amino acid consensus sequence thought to be involved in dolichol recognition. This 13-amino acid sequence is also found in the glycosyltransferase products of genes ALG7 and DPM1, and the product of gene SEC59 [Albright89].
ALG1 mutants accumulated (N-acetylglucosaminyl)2-diphosphodolichol [Huffaker83].
Gene Citations: [Couto84]
Locations: endoplasmic reticulum
|Map Position: [458,866 -> 460,215]|
Molecular Weight of Polypeptide: 51.9 kD (from nucleotide sequence)
|Cellular Component:||GO:0005783 - endoplasmic reticulum [Gao04]|
Enzymatic reaction of: chitobiosyldiphosphodolichol β-mannosyltransferase
EC Number: 188.8.131.52
The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.
The reaction is favored in the direction shown.
In Pathways: dolichyl-diphosphooligosaccharide biosynthesis
The enzyme was partially purified from a solubilized membrane fraction [Sharma82]. Production of mannosyl-(N-acetylglucosaminyl)2-diphosphodolichol was shown in an E. coli expression system [Couto84].
pH(opt): 7.5 [Sharma82]
Albright89: Albright CF, Orlean P, Robbins PW (1989). "A 13-amino acid peptide in three yeast glycosyltransferases may be involved in dolichol recognition." Proc Natl Acad Sci U S A 86(19);7366-9. PMID: 2678101
Albright90: Albright CF, Robbins RW (1990). "The sequence and transcript heterogeneity of the yeast gene ALG1, an essential mannosyltransferase involved in N-glycosylation." J Biol Chem 265(12);7042-9. PMID: 2182636
Couto84: Couto JR, Huffaker TC, Robbins PW (1984). "Cloning and expression in Escherichia coli of a yeast mannosyltransferase from the asparagine-linked glycosylation pathway." J Biol Chem 259(1);378-82. PMID: 6368538
Sato01: Sato M, Fujisaki S, Sato K, Nishimura Y, Nakano A (2001). "Yeast Saccharomyces cerevisiae has two cis-prenyltransferases with different properties and localizations. Implication for their distinct physiological roles in dolichol synthesis." Genes Cells 6(6);495-506. PMID: 11442630
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