EDEM1,3 hydrolyse (GlcNAc)2 (Man)8b to (GlcNAc)2 (Man)5

Stable Identifier
Reaction [omitted]
Homo sapiens
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Proteins with major folding defects are extracted from futile folding cycles in the calnexin chaperone system and the ER Quality Control Compartment, and are translocated back to the cytosol for degradation. The ER degradation-enhancing alpha-mannosidase-like proteins 1 and 3 (EDEM1 and 3) can catalyse the sequential hydrolysis of (GlcNAc)2 (Man)8 to (GlcNAc)2 (Man)7-5. The products are recognised by quality control proteins and become targets for ER-associated degradation (ERAD) (Ninagawa et al. 2014, Hirao et al. 2006).

Literature References
PubMed ID Title Journal Year
25092655 EDEM2 initiates mammalian glycoprotein ERAD by catalyzing the first mannose trimming step

Kamiya, Y, Takeda, S, Ishikawa, T, Sakuma, T, Sumitomo, Y, Okada, T, Yamamoto, T, Horimoto, S, Mori, K, Ninagawa, S, Kato, K

J. Cell Biol. 2014
16431915 EDEM3, a soluble EDEM homolog, enhances glycoprotein endoplasmic reticulum-associated degradation and mannose trimming

Romero, P, Hosokawa, N, Herscovics, A, Wada, I, Nagata, K, Sleno, B, Morito, D, Natsuka, Y, Hirao, K, Tamura, T, Tremblay, LO, Natsuka, S

J Biol Chem 2006
Event Information
Catalyst Activity

mannosyl-oligosaccharide 1,2-alpha-mannosidase activity of EDEM1,3 [endoplasmic reticulum quality control compartment]

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