DOLICHYL-P-GLC:GLC1MAN9GLCNAC2-PP-DOLICHOL ALPHA-1 3-GLUCOSYLTRANSFERASE

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Dolichyl-P-Glc:Glc1Man9GlcNAc2-PP-dolichol alpha-1,3-glucosyltransferase
Dolichyl-P-Glc:Glc1Man9GlcNAc2-PP-dolichol alpha-1,3-glucosyltransferase
Identifiers
EC no.	2.4.1.265
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
PMC
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PMC	articles
PubMed	articles
NCBI	proteins

Dolichyl-P-Glc:Glc1Man9GlcNAc2-PP-dolichol alpha-1,3-glucosyltransferase ( EC 2.4.1.265, ALG8, Dol-P-Glc:Glc1Man9GlcNAc2-PP-Dol alpha-1,3-glucosyltransferase) is an enzyme with systematic name dolichyl beta-D-glucosyl phosphate:D-Glc-alpha-(1->3)-D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-(D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-(D-Man-alpha-(1->2)-D-Man-alpha-(1->6))-D-Man-alpha-(1->6))-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol alpha-1,3-glucosyltransferase.^[1]^[2]^[3]

This enzyme catalyses the following chemical reaction

which is in words:

dolichyl beta-D-glucosyl phosphate + D-Glc-alpha-(1->3)-D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->2)-D-Man-alpha-(1->6)]-D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol

\rightleftharpoons

D-Glc-alpha-(1->3)-D-Glc-alpha-(1->3)-D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->2)-D-Man-alpha-(1->6)]-D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol + dolichyl phosphate

References

^ Stagljar I, te Heesen S, Aebi M (June 1994). "New phenotype of mutations deficient in glucosylation of the lipid-linked oligosaccharide: cloning of the ALG8 locus". Proceedings of the National Academy of Sciences of the United States of America. 91 (13): 5977–81. doi: 10.1073/pnas.91.13.5977. PMC 44120. PMID 8016100.
^ Runge KW, Robbins PW (November 1986). "A new yeast mutation in the glucosylation steps of the asparagine-linked glycosylation pathway. Formation of a novel asparagine-linked oligosaccharide containing two glucose residues". The Journal of Biological Chemistry. 261 (33): 15582–90. doi: 10.1016/S0021-9258(18)66754-7. PMID 3536907.
^ Chantret I, Dancourt J, Dupré T, Delenda C, Bucher S, Vuillaumier-Barrot S, Ogier de Baulny H, Peletan C, Danos O, Seta N, Durand G, Oriol R, Codogno P, Moore SE (March 2003). "A deficiency in dolichyl-P-glucose:Glc1Man9GlcNAc2-PP-dolichyl alpha3-glucosyltransferase defines a new subtype of congenital disorders of glycosylation". The Journal of Biological Chemistry. 278 (11): 9962–71. doi: 10.1074/jbc.M211950200. PMID 12480927.

External links

Dolichyl-P-Glc:Glc1Man9GlcNAc2-PP-dolichol+alpha-1,3-glucosyltransferase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)

[1] Stagljar I, te Heesen S, Aebi M (June 1994). "New phenotype of mutations deficient in glucosylation of the lipid-linked oligosaccharide: cloning of the ALG8 locus". Proceedings of the National Academy of Sciences of the United States of America. 91 (13): 5977–81. doi: 10.1073/pnas.91.13.5977. PMC 44120. PMID 8016100.

[2] Runge KW, Robbins PW (November 1986). "A new yeast mutation in the glucosylation steps of the asparagine-linked glycosylation pathway. Formation of a novel asparagine-linked oligosaccharide containing two glucose residues". The Journal of Biological Chemistry. 261 (33): 15582–90. doi: 10.1016/S0021-9258(18)66754-7. PMID 3536907.

[3] Chantret I, Dancourt J, Dupré T, Delenda C, Bucher S, Vuillaumier-Barrot S, Ogier de Baulny H, Peletan C, Danos O, Seta N, Durand G, Oriol R, Codogno P, Moore SE (March 2003). "A deficiency in dolichyl-P-glucose:Glc1Man9GlcNAc2-PP-dolichyl alpha3-glucosyltransferase defines a new subtype of congenital disorders of glycosylation". The Journal of Biological Chemistry. 278 (11): 9962–71. doi: 10.1074/jbc.M211950200. PMID 12480927.

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v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases ( list) EC2 Transferases ( list) EC3 Hydrolases ( list) EC4 Lyases ( list) EC5 Isomerases ( list) EC6 Ligases ( list) EC7 Translocases ( list)

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases ( list) EC2 Transferases ( list) EC3 Hydrolases ( list) EC4 Lyases ( list) EC5 Isomerases ( list) EC6 Ligases ( list) EC7 Translocases ( list)

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