2.5.1.87: ditrans,polycis-polyprenyl diphosphate synthase [(2E,6E)-farnesyl diphosphate specific]
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For detailed information about ditrans,polycis-polyprenyl diphosphate synthase [(2E,6E)-farnesyl diphosphate specific], go to the full flat file.
Word Map on EC 2.5.1.87
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2.5.1.87
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dolichols
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cis-prenyltransferase
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pigmentosa
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dehydrodolichol
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jewish
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nogos
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myoclonus
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ashkenazi
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npc2
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polyprenols
- 2.5.1.87
- dolichols
- cis-prenyltransferase
- pigmentosa
- dehydrodolichol
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jewish
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nogos
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myoclonus
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ashkenazi
- npc2
- polyprenols
Reaction
+ n isopentenyl diphosphate = n diphosphate +
Synonyms
AcpT, anther-66, cis-prenyltransferase, cis-PTase, CPT1, Dedol-PP synthase, DedolPP synthase, dehydrodolichyl diphosphate synthase, dehydrodolichyl diphosphate synthase 1, DHDDS, NgBR, Nogo-B receptor, RER2, Rer2p, Rer2p Z-prenyltransferase, SlCPT3, SRT1, Srt1p, Srt2p Z-prenyltransferase, Tk-IdsB
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General Information
General Information on EC 2.5.1.87 - ditrans,polycis-polyprenyl diphosphate synthase [(2E,6E)-farnesyl diphosphate specific]
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evolution
malfunction
metabolism
physiological function
amino acid at 4th position from the C-terminus of NgBR is a functionally and evolutionary conserved residue
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
evolution
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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
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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
malfunction
the morphological differentiation of a Candida albicans cis-prenyltransferase mutant is impaired
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
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
malfunction
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the morphological differentiation of a Candida albicans cis-prenyltransferase mutant is impaired
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cis-Prenyltransferase is the first enzyme of the mevalonate pathway committed to the biosynthesis of dolichol in eukaryotes
metabolism
necessity of both dehydrodolichol diphosphate synthase, DHDDS or hCIT, and Nogo-B receptor, NgBR, for dolichol biosynthesis
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
metabolism
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cis-Prenyltransferase is the first enzyme of the mevalonate pathway committed to the biosynthesis of dolichol in eukaryotes
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dehydrodolichyl diphosphate synthase catalyzes the sequential condensation of isopentenyl diphosphate with farnesyl diphosphate to synthesize dehydrodolichyl diphosphate, a biosynthetic precursor for dolichol which plays an important role as a sugar-carrier lipid in the biosynthesis of glycoprotein in eukaryotic cells. Identification of a specific interaction of human dehydrodolichyl diphosphate synthase with the NiemannPick Type C2 protein (NPC2/HE1), whose defects cause NiemannPick type C2 disease
physiological function
involved in biosynthesis of dolichol (a long-chain polyprenol with a saturated alpha-isoprene unit, which serves as a glycosyl carrier in protein glycosylation). Of the two isozymes, Rer2p and Srt1p, isoenzyme Rer2p is responsible for the main activity of the wild-type cells, and the expression of RER2 is highest in the early logarithmic phase when the cells are actively dividing
physiological function
key enzyme in dolichol biosynthesis, the identity of the cloned enzyme is confirmed by functional complementation of a yeast mutant strain defective in dehydrodolichyl-diphosphates synthase activity, Arabidopsis thaliana enzyme catalyzes the synthesis of dehydrodolichyl-diphosphates with chain lengths similar to those found in yeast
physiological function
over-expression of SRT1 suppresses the growth and glycosylation defects of rer2. SRT1 has only a minor contribution to total cis-prenyltransferase activity under normal conditions
physiological function
RER2 encodes a key enzyme of dolichol synthesis
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
physiological function
cis-prenyltransferase is committed to the synthesis of dolichol, the Nogo-B receptor, NgBR, is a subunit required for dolichol synthesis in mice, essential role of NgBR in dolichol synthesis and protein glycosylation
physiological function
cis-prenyltransferase Rer2 is required for protein glycosylation, cell wall integrity and hypha formation. Dolichols are essential not only for protein glycosylation and cell wall integrity but also for growth and development of Candida albicans
physiological function
the SlCPT3 and SlCPTBP proteins interact to form a functional dolichol synthase
physiological function
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cis-prenyltransferase Rer2 is required for protein glycosylation, cell wall integrity and hypha formation. Dolichols are essential not only for protein glycosylation and cell wall integrity but also for growth and development of Candida albicans
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physiological function
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the SlCPT3 and SlCPTBP proteins interact to form a functional dolichol synthase
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