Farnesyl-diphosphate farnesyltransferase 1: Difference between revisions
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'''Farnesyl-diphosphate farnesyltransferase 1''' is a [[protein]] that in humans is encoded by the FDFT1 [[gene]]. | '''[[Farnesyl-diphosphate farnesyltransferase]] 1''' is a [[protein]] that in humans is encoded by the FDFT1 [[gene]]. | ||
<ref name="entrez"> | <ref name="entrez"> | ||
{{cite web | {{cite web | ||
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==Function== | ==Function== | ||
This gene encodes a membrane-associated enzyme located at a branch point in the mevalonate pathway. The encoded protein is the first specific enzyme in cholesterol biosynthesis, catalyzing the dimerization of two molecules of farnesyl diphosphate in a two-step reaction to form squalene. | This gene encodes a membrane-associated [[enzyme]] located at a branch point in the [[mevalonate pathway]]. The encoded protein is the first specific enzyme in cholesterol biosynthesis, catalyzing the dimerization of two molecules of [[Farnesyl pyrophosphate|farnesyl diphosphate]] in a two-step reaction to form [[squalene]]. | ||
== References == | == References == | ||
Revision as of 00:08, 7 April 2018
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| External IDs | GeneCards: [1] | ||||||
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| Location (UCSC) | n/a | n/a | |||||
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Farnesyl-diphosphate farnesyltransferase 1 is a protein that in humans is encoded by the FDFT1 gene. [1]
Function
This gene encodes a membrane-associated enzyme located at a branch point in the mevalonate pathway. The encoded protein is the first specific enzyme in cholesterol biosynthesis, catalyzing the dimerization of two molecules of farnesyl diphosphate in a two-step reaction to form squalene.
References
- ↑ "Entrez Gene: Farnesyl-diphosphate farnesyltransferase 1". Retrieved 2016-06-25.
Further reading
- Kavanagh KL, Guo K, Dunford JE, Wu X, Knapp S, Ebetino FH, Rogers MJ, Russell RG, Oppermann U (2006). "The molecular mechanism of nitrogen-containing bisphosphonates as antiosteoporosis drugs". Proc. Natl. Acad. Sci. U.S.A. 103 (20): 7829–34. doi:10.1073/pnas.0601643103. PMC 1472530. PMID 16684881.
This article incorporates text from the United States National Library of Medicine, which is in the public domain.
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