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PMID: 10542413 Published · ppublish English Journal Article Review

Chain-length determination mechanism of isoprenyl diphosphate synthases and implications for molecular evolution.

Trends in biochemical sciences ·Vol. 24 ·No. 11 ·1999-11-00 ·Pages 445-51

Wang K, Ohnuma S

Abstract

In the synthesis of isoprenoids, isoprenyl diphosphate synthases catalyze the consecutive condensation of isopentenyl diphosphate with allylic diphosphates to produce a variety of prenyl diphosphates with well-defined chain lengths. Site-directed mutagenesis in conjunction with X-ray crystallographic studies have identified specific amino acid residues responsible for chain-length determination. Simple combinations of these residues within a characteristic motif are not only sufficient to confer product specificities to all isoprenyl diphosphate synthases but represent structural features that reflect the enzyme family's evolutionary course.

MeSH Terms
Alkyl and Aryl Transferases/chemistry,genetics,metabolism Amino Acid Sequence Animals Conserved Sequence/genetics Evolution, Molecular Farnesyltranstransferase Genetic Variation/genetics Humans Molecular Weight Phylogeny Protein Conformation
Chemicals
Alkyl and Aryl Transferases Farnesyltranstransferase
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Wang K
University of California San Francisco, School of Medicine, S 245, Box 0454, San Francisco, CA 94143, USA.
Ohnuma S
Article Info
Journal
Trends in biochemical sciences
Abbr.
Trends Biochem Sci
ISSN
0968-0004
Published
1999-11-00
Pages
445-51
Language
English
Region
England
NLM ID
7610674
Subset
IM
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