| Entry |
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| Name |
dolichyl-P-Man:Man5GlcNAc2-PP-dolichol alpha-1,3-mannosyltransferase;
Man5GlcNAc2-PP-Dol mannosyltransferase;
ALG3;
dolichyl-P-Man:Man(5)GlcNAc(2)-PP-dolichyl mannosyltransferase;
Not56-like protein;
Alg3 alpha-1,3-mannosyl transferase;
Dol-P-Man:Man5GlcNAc2-PP-Dol alpha-1,3-mannosyltransferase
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| Class |
Transferases;
Glycosyltransferases;
Hexosyltransferases
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| Sysname |
dolichyl beta-D-mannosyl phosphate:D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol alpha-1,3-mannosyltransferase
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| Reaction(IUBMB) |
dolichyl beta-D-mannosyl phosphate + D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol = D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->3)-D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol + dolichyl phosphate [RN: R06258]
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| Reaction(KEGG) |
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| Substrate |
dolichyl beta-D-mannosyl phosphate;
D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol
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| Product |
D-Man-alpha-(1->2)-D-Man-alpha-(1->2)-D-Man-alpha-(1->3)-[D-Man-alpha-(1->3)-D-Man-alpha-(1->6)]-D-Man-beta-(1->4)-D-GlcNAc-beta-(1->4)-D-GlcNAc-diphosphodolichol;
dolichyl phosphate [CPD: C00110]
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| Comment |
The formation of N-glycosidic linkages of glycoproteins involves the ordered assembly of the common Glc3Man9GlcNAc2 core-oligosaccharide on the lipid carrier dolichyl diphosphate. Early mannosylation steps occur on the cytoplasmic side of the endoplasmic reticulum with GDP-Man as donor, the final reactions from Man5GlcNAc2-PP-dolichol to Man9Glc-NAc2-PP-dolichol on the lumenal side use dolichyl beta-D-mannosyl phosphate. The first step of this assembly pathway on the luminal side of the endoplasmic reticulum is catalysed by ALG3.
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| Pathway |
| N-Glycan biosynthesis | | Various types of N-glycan biosynthesis | | Metabolic pathways |
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| Orthology |
| alpha-1,3-mannosyltransferase |
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| Genes |
HSA: | | PTR: | | PPS: | | GGO: | | PON: | | MCC: | | MMU: | | RNO: | | CFA: | | AML: | | FCA: | | BTA: | | SSC: | | ECB: | | MDO: | | SHR: | | OAA: | | GGA: | | MGP: | | TGU: | | ACS: | | XLA: | | XTR: | | DRE: | | TRU: | | OLA: | | BFO: | | CIN: | | SPU: | | DME: | | DPO: | | DAN: | | DER: | | DPE: | | DSE: | | DSI: | | DWI: | | DYA: | | DGR: | | DMO: | | DVI: | | AGA: | | AAG: | | CQU: | | AME: | | NVI: | | TCA: | | PHU: | | ISC: | | CBR: | | TSP: | | SMM: | | NVE: | | HMG: | | AQU: | | ATH: | | ALY: | | GMX: | | MTR: | | CSV: | | RCU: | | POP: | | VVI: | | DOSA: | | BDI: | | SBI: | | ZMA: | | SMO: | | PPP: | | OLU: | | CME: | | SCE: | | AGO: | | ERC: | | KLA: | | LTH: | | PPA: | | VPO: | | ZRO: | | CGR: | | NCS: | | NDI: | | TPF: | | TBL: | | TDL: | | KAF: | | DHA: | | PIC: | | PGU: | | LEL: | | CAL: | | CTP: | | CDU: | | COT: | | YLI: | | CLU: | | NCR: | | SMP: | | PAN: | | TTT: | | MTM: | | FGR: | | NHE: | | VAL: | | SSL: | | BFU: | | ANI: | | NFI: | | AFM: | | AOR: | | ACT: | | PCS: | | CIM: | | CPW: | | PBL: | | URE: | | ABE: | | TVE: | | AJE: | | PTE: | | ZTR: | | TML: | | SPO: | | CNE: | | CNB: | | CGI: | | LBC: | | MPR: | | CCI: | | SCM: | | PGR: | | MBR: | | DDI: | | DPP: | | TBR: | | TCR: | | LMA: | | LIF: | | LDO: | | LMI: | | LBZ: | | PTI: | | TPS: | |
» show all
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| Reference |
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| Authors |
Sharma CB, Knauer R, Lehle L |
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| Title |
Biosynthesis of lipid-linked oligosaccharides in yeast: the ALG3 gene encodes the Dol-P-Man:Man5GlcNAc2-PP-Dol mannosyltransferase. |
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| Journal |
Biol. Chem. 382 (2001) 321-8. |
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| Organism |
Saccharomyces cerevisiae [GN: sce] |
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| Reference |
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| Authors |
Cipollo JF, Trimble RB |
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| Title |
The accumulation of Man(6)GlcNAc(2)-PP-dolichol in the Saccharomyces cerevisiae Deltaalg9 mutant reveals a regulatory role for the Alg3p alpha1,3-Man middle-arm addition in downstream oligosaccharide-lipid and glycoprotein glycan processing. |
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| Journal |
J. Biol. Chem. 275 (2000) 4267-77. |
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| Organism |
Saccharomyces cerevisiae [GN: sce] |
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| Other DBs |
ExplorEnz - The Enzyme Database: IUBMB Enzyme Nomenclature: ExPASy - ENZYME nomenclature database: BRENDA, the Enzyme Database: |
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