Isopentenyl Diphosphate Isomerase: A Checkpoint to Isoprenoid Biosynthesis

Biochimie. 2012 Aug;94(8):1621-34. doi: 10.1016/j.biochi.2012.03.021. Epub 2012 Apr 4.

Abstract

Even if the isopentenyl diphosphate (IPP) isomerases have been discovered in the 50s, it is only in the last decade that the genetical, enzymatical, structural richness and cellular importance of this large family of crucial enzymes has been uncovered. Present in all living kingdoms, they can be classified in two subfamilies: type 1 and type 2 IPP isomerases, which show clearly distinct characteristics. They all perform the regulatory isomerization of isopentenyl diphosphate into dimethylallyl diphosphate, a key rate-limiting step of the terpenoid biosynthesis, via a protonation/deprotonation mechanism. Due to their importance in the isoprenoid metabolism and the increasing interest of industry devoted to terpenoid production, it is foreseen that the biotechnological development of such enzymes should be under intense scrutiny in the near future.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Carbon-Carbon Double Bond Isomerases / chemistry*
  • Carbon-Carbon Double Bond Isomerases / classification
  • Carbon-Carbon Double Bond Isomerases / genetics*
  • Carbon-Carbon Double Bond Isomerases / metabolism
  • Catalysis
  • Hemiterpenes / chemistry
  • Humans
  • Molecular Conformation
  • Molecular Sequence Data
  • Organophosphorus Compounds / chemistry
  • Phylogeny
  • Plants / enzymology*
  • Terpenes / chemistry*
  • Terpenes / metabolism

Substances

  • Hemiterpenes
  • Organophosphorus Compounds
  • Terpenes
  • isopentenyl pyrophosphate
  • Carbon-Carbon Double Bond Isomerases
  • isopentenyldiphosphate delta-isomerase