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

Stable Identifier
Reaction [transition]
Homo sapiens
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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
20080937 A severe human metabolic disease caused by deficiency of the endoplasmatic mannosyltransferase hALG11 leads to congenital disorder of glycosylation-Ip

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

Hum. Mol. Genet. 2010
22213132 Improved diagnostics lead to identification of three new patients with congenital disorder of glycosylation-Ip

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

Hum. Mutat. 2012
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]

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