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Purification and characterization of human dehydrodolychil diphosphate synthase (DHDDS) overexpressed in E. coli.

Protein Expr Purif.. 2017-02; 
Giladi M, Edri I, Goldenberg M, Newman H, Strulovich R, Khananshvili D, Haitin Y, Loewenstein A. Department of Physiology and Pharmacology, Sackler Faculty of Medicine, Tel Aviv University, Tel Aviv, Israel.
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Abstract

Protein asparagine (N)-linked glycosylation is a post-translational modification that occurs in the endoplasmic reticulum; it plays an important role in protein folding, oligomerization, quality control, sorting, and transport. Accordingly, disorders of glycosylation may affect practically every organ system. Dehydrodolichyl diphosphate synthase (DHDDS) is an eukaryotic cis prenyltransferase (cis-PT) that catalyzes chain elongation of farnesyl diphosphate via multiple condensations with isopentenyl diphosphate to form dehydrodolichyl diphosphate, a precursor for the glycosyl carrier dolichylpyrophophate involved in N-linked glycosylation. Mutations in DHDDS were shown to result in retinitis pigmentosa, ultimate... More

Keywords

DHDDS; Dehydrodolychil diphosphate synthase; Dolichol; Enzyme; Heterologous expression; Prenyltransferase