Related Experiment Video
Updated: Aug 8, 2026

Optimization of Synthetic Proteins: Identification of Interpositional Dependencies Indicating Structurally and/or Functionally Linked Residues
Published on: July 14, 2015
Chain-length determination mechanism of isoprenyl diphosphate synthases and implications for molecular evolution
1University of California San Francisco, School of Medicine, S 245, Box 0454, San Francisco, CA 94143, USA.
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.
Related Concept Videos
Bacterial RNA Polymerase
In most genes, the transcription site is a single base present upstream of the coding sequence. Though RNAP is a catalytically efficient enzyme, it does not recognize...
ATP Synthase: Mechanism
ATP Synthase: Structure
Bacterial Transcription
Transcription can be divided into three main stages, each involving distinct DNA sequences to guide the polymerase. These are:
Biosynthesis of Polysaccharides
Biosynthesis of Lipids

