Defective ALG11 does not transfer Man to the N-glycan precursor

Stable Identifier
R-HSA-4551297
Type
Reaction [transition]
Species
Homo sapiens
Compartment
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GDP-Man:Man(3)GlcNAc(2)-PP-Dol alpha-1,2-mannosyltransferase (ALG11) transfers the fourth and fifth mannoses (Man) to the N-glycan precursor in an alpha-1,2 orientation. These additions are the last two on the cytosolic side of the ER membrane before the N-glycan is flipped to the luminal side of the membrane. Recently discovered defects in ALG11 have been linked to congential disorder of glycosylation, type 1p (ALG11-CDG, CGD1p) (Rind et al. 2010, Thiel et al. 2012). The disease is a multi-system disorder characterised by under-glycosylated serum glycoproteins. Mutations causing ALG11-CDG include E398K, L381S, L86S, Q318P and Y279S (Rind et al. 2010, Thiel et al. 2012).

Literature References
PubMed ID Title Journal Year
22213132 Improved diagnostics lead to identification of three new patients with congenital disorder of glycosylation-Ip

Thiel, C, Rind, N, Popovici, D, Hoffmann, GF, Hanson, K, Conway, RL, Adamski, CR, Butler, E, Scanlon, R, Lambert, M, Apeshiotis, N, Thiels, C, Matthijs, G, Körner, C

Hum. Mutat. 2012
20080937 A severe human metabolic disease caused by deficiency of the endoplasmatic mannosyltransferase hALG11 leads to congenital disorder of glycosylation-Ip

Rind, N, Schmeiser, V, Thiel, C, Absmanner, B, Lübbehusen, J, Hocks, J, Apeshiotis, N, Wilichowski, E, Lehle, L, Körner, C

Hum. Mol. Genet. 2010
Participants
Participates
Catalyst Activity

alpha-1,2-mannosyltransferase activity of ALG11 mutants [endoplasmic reticulum membrane]

Normal reaction
Functional status

Loss of function of ALG11 mutants [endoplasmic reticulum membrane]

Status
Authored
Reviewed
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