Chain elongation in the isoprenoid biosynthetic pathway.
Isoprenyl diphosphate synthases catalyze addition of allylic diphosphate primers to the isoprene unit in isopentenyl diphosphate to produce polyisoprenoid diphosphates with well defined chain lengths. Phylogenetic correlations suggest that the synthases which catalyze formation of isoprenoid diphosphates with (E) double bonds have evolved from a common ancestor. X-ray crystallographic studies of farnesyl diphosphate synthase in conjunction with site-directed mutagenesis have provided important new information about the residues involved in binding and catalysis and the source of chain length selectivity for the enzymes that catalyze chain elongation.
Kellogg
B A
BA
Department of Chemistry, University of Utah, Salt Lake City, UT 84112, USA.
Poulter
C D
CD
D019883:Alkyl and Aryl Transferases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D001665:Binding Sites; D002384:Catalysis; D019281:Dimerization; D051231:Farnesyltranstransferase; D051228:Geranyltranstransferase; D008958:Models, Molecular; D008968:Molecular Conformation; D015394:Molecular Structure; D010802:Phylogeny; D011106:Polyisoprenyl Phosphates / Q000096:biosynthesis* / Q000737:chemistry; D017368:Protein Prenylation; D017433:Protein Structure, Secondary; D012441:Saccharomyces cerevisiae / Q000201:enzymology / Q000235:genetics
D011106:Polyisoprenyl Phosphates; D019883:Alkyl and Aryl Transferases; D051228:Geranyltranstransferase; D051231:Farnesyltranstransferase