Reactome | Addition of a third mannose to the N-glycan precursor by ALG2

Addition of a third mannose to the N-glycan precursor by ALG2

Stable Identifier

R-HSA-449718

Type

Reaction [transition]

Species

Homo sapiens

Compartment

endoplasmic reticulum membrane

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Addition of a third mannose to the N-glycan precursor by ALG2

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A third mannose is added to the N-glycan precursor by ALG2 using its alpha1,6-mannosyltransferase activity. This has been demonstrated experimentally in yeast (O'Reilly MK et al, 2006; Kämpf M et al, 2009); the human reaction is inferred by homology. Defects in ALG2 are the cause for CDG1I (Thiel C et al, 2003).

Literature References

PubMed ID	Title	Journal	Year
16878994	In vitro evidence for the dual function of Alg2 and Alg11: essential mannosyltransferases in N-linked glycoprotein biosynthesis O'Reilly, MK, Zhang, G, Imperiali, B	Biochemistry	2006
19282279	Biochemical characterization and membrane topology of Alg2 from Saccharomyces cerevisiae as a bifunctional alpha1,3- and 1,6-mannosyltransferase involved in lipid-linked oligosaccharide biosynthesis Kämpf, M, Absmanner, B, Schwarz, M, Lehle, L	J Biol Chem	2009
12684507	A new type of congenital disorders of glycosylation (CDG-Ii) provides new insights into the early steps of dolichol-linked oligosaccharide biosynthesis Thiel, C, Schwarz, M, Peng, J, Grzmil, M, Hasilik, M, Braulke, T, Kohlschütter, A, von Figura, K, Lehle, L, Körner, C	J Biol Chem	2003

Participants

Input

Output

Participant Of

hasEvent

Biosynthesis of the N-glycan precursor (dolichol lipid-linked oligosaccharide, LLO) and transfer to a nascent protein

Catalyst Activity

Title

alpha-1,6-mannosyltransferase activity of ALG2 [endoplasmic reticulum membrane]

Physical Entity

ALG2 [endoplasmic reticulum membrane]

Activity

alpha-1,6-mannosyltransferase activity (0000009)

Inferred From

Addition of a third mannose to the N-glycan precursor by Alg2 (Saccharomyces cerevisiae)

Authored

Dall'Olio, GM (2009-11-10)

Reviewed

Gagneux, P (2010-04-16)

Created

Jassal, B (2009-12-07)