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Asn glycosylation
N-glycosylation is conserved from yeast to humans.
Glycoprotein profiling of N-glycans may be facilitated by DSA-FACE. [1]
Activated core oligosaccharide of dolichol pyrophosphate transfered enbloc to a specific asparigine residue of growing ER & GOLGI-processed proteins within the lumen of the endoplasmic reticulum.
* see figure
Biochemistry:
- Asn glycosylation 1
- enzyme: transferase (cytoplasm)
- substrate: dolichol phosphate (ER) + UDP N-acetylglucosamine (cytoplasm))
- product: dolichol pyrophosphate-GlcNAc (ER) + UMP
- Asn glycosylation 2
- enzyme: transferase
- substrate: dolicholpyrophosphate-GlcNAc + UDP N-acetylglucosamine
- product: dolichol pyrophosphate-[GlcNAc]2 +UDP
- reaction on cytoplasmic face of endoplasmic reticulum (ER)
- Asn glycosylation 3
- enzyme: transferase
- substrate: dolichol pyrophosphate-[GlcNAc]2 + 5 GDP-mannose
- product: dolichol pyrophosphate-[GlcNAc]2-[Man]5 + 5 GDP
- reaction on cytoplasmic face of endoplasmic reticulum (ER)
- Asn glycosylation 4
- substrate: dolichol pyrophosphate-[GlcNAc]2-[Man]5
- product: dolichol pyrophosphate-[GlcNAc]2-[Man]5
- translocation from cytoplasmic face to luminal face of ER
- Asn glycosylation 5
- enzyme: transferase
- substrate: dolichol pyrophosphate-[GlcNAc]2-[Man]5 + 4 dolichol phosphate-Man
- product: dolichol pyrophosphate-[GlcNAc]2-[Man]9 + dolichol phosphate
- reaction on luminal face of endoplasmic reticulum (ER)
- Asn glycosylation 6
- enzyme: transferase
- substrate: dolichol pyrophosphate-[GlcNAc]2-[Man]9 + 3 dolicholphosphate-Glc
- product: dolichol pyrophosphate-[GlcNAc]2-[Man]9-[Glc]3 + 3 dolichol phosphate
- reaction on luminal face of endoplasmic reticulum (ER)
- Asn glycosylation 7
- enzyme: transferase
- substrate: dolichol pyrophosphate-[GlcNAc]2-[Man]9-[Glc]3 + glycoprotein
- product: glycoprotein with core oligosaccharide + dolichol pyrophosphate
- N-glycosylated glycoprotein with core oligosaccharide in endoplasmic reticulum
Related
N-glycosylation site or Asn glycosylation site
General
protein glycosylation
Properties
EVENTS:
enzymatic reaction
ENZYME: transferase
COMPARTMENT: cytoplasm
MOTIF: active site
SUBSTRATE: dolichol phosphate
COMPARTMENT: endoplasmic reticulum
UDP N-acetylglucosamine
COMPARTMENT: cytoplasm
PRODUCT: dolichol pyrophosphate NAc-glucose
COMPARTMENT: endoplasmic reticulum
EFFECTOR-BOUND: N-acetylglucosamine
uridine monophosphate
TAG: ASN-GLYCOSYLATION-1
enzymatic reaction
ENZYME: transferase
COMPARTMENT: cytoplasm
MOTIF: active site
SUBSTRATE: dolichol pyrophosphate
COMPARTMENT: endoplasmic reticulum
EFFECTOR-BOUND: UDP N-acetylglucosamine
COMPARTMENT: cytoplasm
UDP N-acetylglucosamine
COMPARTMENT: cytoplasm
PRODUCT: dolichol pyrophosphate-[GlcNAc]2
COMPARTMENT: endoplasmic reticulum
EFFECTOR-BOUND: [GLCNAC]2
uridine diphosphate
TAG: ASN-GLYCOSYLATION-2
enzymatic reaction
ENZYME: transferase
COMPARTMENT: cytoplasm
MOTIF: active site
SUBSTRATE: dolichol pyrophosphate-[GlcNAc]2
COMPARTMENT: endoplasmic reticulum
EFFECTOR-BOUND: [GLCNAC]2
GDP mannose (5)
COMPARTMENT: cytoplasm
PRODUCT: dolichol pyrophosphate-[GlcNAc]2-[Man]5
COMPARTMENT: endoplasmic reticulum
EFFECTOR-BOUND: [GLCNAC]2-[MAN]5
guanosine diphosphate (5)
TAG: ASN-GLYCOSYLATION-3
enzymatic reaction
ENZYME: enzyme
MOTIF: active site
SUBSTRATE: dolichol pyrophosphate-[GlcNAc]2-[Man]5
COMPARTMENT: endoplasmic reticulum
EFFECTOR-BOUND: [GLCNAC]2-[MAN]5
PRODUCT: dolichol pyrophosphate-[GlcNAc]2-[Man]5
COMPARTMENT: endoplasmic reticulum
EFFECTOR-BOUND: [GLCNAC]2-[MAN]5
TAG: ASN-GLYCOSYLATION-4
enzymatic reaction
ENZYME: transferase
COMPARTMENT: endoplasmic reticulum
MOTIF: active site
SUBSTRATE: dolichol pyrophosphate-[GlcNAc]2-[Man]5
COMPARTMENT: endoplasmic reticulum
EFFECTOR-BOUND: [GLCNAC]2-[MAN]5
dolichol phosphate mannose (4)
COMPARTMENT: endoplasmic reticulum
EFFECTOR-BOUND: mannose
PRODUCT: dolichol pyrophosphate-[GlcNAc]2-[Man]9
COMPARTMENT: endoplasmic reticulum
EFFECTOR-BOUND: [GLCNAC]2-[MAN]9
dolichol phosphate (4)
COMPARTMENT: endoplasmic reticulum
TAG: ASN-GLYCOSYLATION-5
enzymatic reaction
ENZYME: transferase
COMPARTMENT: endoplasmic reticulum
MOTIF: active site
SUBSTRATE: dolichol pyrophosphate-[GlcNAc]2-[Man]9
COMPARTMENT: endoplasmic reticulum
EFFECTOR-BOUND: [GLCNAC]2-[MAN]9
dolichol phosphate glucose (3)
COMPARTMENT: endoplasmic reticulum
EFFECTOR-BOUND: gas-liquid chromatography
PRODUCT: dolichol pyrophosphate-[GlcNAc]2-[Man]9-[Glc]3
COMPARTMENT: endoplasmic reticulum
EFFECTOR-BOUND: [GLCNAC]2-[MAN]9-[GLC]3
dolichol phosphate (3)
COMPARTMENT: endoplasmic reticulum
TAG: ASN-GLYCOSYLATION-6
enzymatic reaction
ENZYME: transferase
COMPARTMENT: endoplasmic reticulum
MOTIF: active site
SUBSTRATE: dolichol pyrophosphate-[GlcNAc]2-[Man]9-[Glc]3
COMPARTMENT: endoplasmic reticulum
EFFECTOR-BOUND: [GLCNAC]2-[MAN]9-[GLC]3
glycoprotein
COMPARTMENT: endoplasmic reticulum
MOTIF: glycosylation site
PRODUCT: glycoprotein
COMPARTMENT: endoplasmic reticulum
MOTIF: N-glycosylation site
MODIFICATION: CORE-OLIGOSACCHARIDE
dolichol pyrophosphate
COMPARTMENT: endoplasmic reticulum
TAG: ASN-GLYCOSYLATION-7
References
- Chen C, Desmyter, L, Van Moller W, de Cabo R, Laroy W, Libert,
Contreras R, Glycoprofiling of serum N-glycans: a potential
aging biomarker.
Aging: Mechanisms and Prevention
34th Annual Meeting of the American Aging Association
June 3-6, 2005, Oakland CA