EC Number   |
General Information |
Reference |
|---|
    2.5.1.87 | evolution |
amino acid at 4th position from the C-terminus of NgBR is a functionally and evolutionary conserved residue |
738001 |
| 2.5.1.87 | evolution |
the class of enzymes known as cis-prenyltransferases (CPTs) elongate the trans-prenyl diphosphate intermediate with a cis-linked linear polymer of isopentenyl diphosphate units |
-, 739317 |
| 2.5.1.87 | malfunction |
rer2 mutant is defective in both N- and O-linked glycosylation in the endoplasmic reticulum, the rer2 mutant is deficient in the activity of cis-prenyltransferase, a key enzyme of dolichol synthesis |
705681 |
| 2.5.1.87 | malfunction |
the morphological differentiation of a Candida albicans cis-prenyltransferase mutant is impaired |
-, 738313 |
| 2.5.1.87 | malfunction |
unique congenital disorder of glycosylation caused by a mutation in NgBR, a conserved subunit of cis-PTase. The disorder of glycosylation is caused by a loss-of-function mutation R290H in the conserved C-terminus of NgBR protein, fibroblasts isolated from patients exhibit reduced dolichol profiles. Mutation of NgBR-R290H in humans show the importance of the evolutionarily conserved residue R290 for mammalian cis-PTase activity and function |
738001 |
| 2.5.1.87 | malfunction |
unique congenital disorder of glycosylation caused by a mutation in NgBR, a conserved subunit of cis-PTase. The disorder of glycosylation is caused by a loss-of-function mutation R290H in the conserved C-terminus of NgBR protein, fibroblasts isolated from patients exhibit reduced dolichol profiles. Mutation of NgBR-R290H in humans show the importance of the evolutionarily conserved residue R290 for mammalian cis-PTase activity and function. SRD5A3-CDG affects the final step in dolichol synthesis. Its clinical features are typical for CDG type 1 glycosylation disorders including psychomotor retardation, ocular malformations, cerebellar hypoplasia, skin lesions, and facial dysmorphism |
738001 |
| 2.5.1.87 | metabolism |
cis-Prenyltransferase is the first enzyme of the mevalonate pathway committed to the biosynthesis of dolichol in eukaryotes |
-, 738313 |
| 2.5.1.87 | metabolism |
necessity of both dehydrodolichol diphosphate synthase, DHDDS or hCIT, and Nogo-B receptor, NgBR, for dolichol biosynthesis |
738001 |
| 2.5.1.87 | metabolism |
necessity of both dehydrodolichol diphosphate synthase, DHDDS or hCIT, and Nogo-B receptor, NgBR, for dolichol biosynthesis. Single subunit cis-PTases catalyze the condensation reactions of isopentenyl diphosphate (IPP) with farnesyl diphosphate (FPP) to synthesize linear polyprenyl diphosphate with specific chain lengths. Polyprenyl pyrophosphate is dephosphorylated into polyprenol and then reduced by a polyprenol reductase to produce dolichol |
738001 |
| 2.5.1.87 | physiological function |
cis-prenyltransferase is committed to the synthesis of dolichol, the Nogo-B receptor, NgBR, is a subunit required for dolichol synthesis in humans, essential role of NgBR in dolichol synthesis and protein glycosylation. NgBR as a protein interacts with reticulon 4B, also called Nogo-B |
738001 |
