Fusicocca-2,10(14)-diene synthase
class of enzymes
Fusicocca-2,10(14)-diene synthase (EC 4.2.3.43, fusicoccadiene synthase, PaFS, PaDC4) is an enzyme with systematic name geranylgeranyl diphosphate-lyase (fusicocca-2,10(14)-diene-forming). This enzyme catalyses the following chemical reaction
geranylgeranyl diphosphate
⇌
{\displaystyle \rightleftharpoons }
fusicocca-2,10(14)-diene + diphosphate
This multifunctional enzyme also has EC 2.5.1.29, farnesyltranstransferase, activity. In 2016, the crystal structures of individual prenyltransferase and cyclase domains were reported by the research group of David W. Christianson at the University of Pennsylvania. The structure of the intact, full-length enzyme was studied using negative-stain electron microscopy and cryo-electron microscopy, showing that a central prenyltransferase octamer was surrounded by eight randomly splayed-out cyclase domains capable of transient association with the prenyltransferase.
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This entry incorporates text from “Fusicocca-2,10(14)-diene synthase” on English Wikipedia. Contributors are listed in the page history. Text is available under the Creative Commons Attribution-ShareAlike 4.0 License. Selected authority identifiers and statements are retrieved from Wikidata under CC0; their references and qualifiers remain part of the verification path.