Studies on the nonmevalonate terpene biosynthetic pathway: metabolic role of IspH (LytB) protein

Proc Natl Acad Sci U S A. 2002 Feb 5;99(3):1158-63. doi: 10.1073/pnas.032658999. Epub 2002 Jan 29.

Abstract

Isopentenyl diphosphate and dimethylallyl diphosphate serve as the universal precursors for the biosynthesis of terpenes. Although their biosynthesis by means of mevalonate has been studied in detail, a second biosynthetic pathway for their formation by means of 1-deoxy-D-xylulose 5-phosphate has been discovered only recently in plants and certain eubacteria. Earlier in vivo experiments with recombinant Escherichia coli strains showed that exogenous 1-deoxy-D-xylulose can be converted into 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate by the consecutive action of enzymes specified by the xylB and ispCDEFG genes. This article describes the transformation of exogenous [U-(13)C(5)]1-deoxy-D-xylulose into a 5:1 mixture of [U-(13)C(5)]isopentenyl diphosphate and [U-(13)C(5)]dimethylallyl diphosphate by an E. coli strain engineered for the expression of the ispH (lytB) gene in addition to recombinant xylB and ispCDEFG genes.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins / genetics
  • Bacterial Proteins / metabolism*
  • Base Sequence
  • Enterobacteriaceae / genetics
  • Escherichia coli / genetics*
  • Escherichia coli / metabolism
  • Escherichia coli Proteins*
  • Magnetic Resonance Spectroscopy
  • Mevalonic Acid / metabolism*
  • Molecular Sequence Data
  • Mycobacterium tuberculosis / genetics
  • Oligodeoxyribonucleotides / chemistry
  • Operon*
  • Oxidoreductases*
  • Promoter Regions, Genetic
  • Recombinant Proteins / metabolism
  • Terpenes / metabolism*

Substances

  • Bacterial Proteins
  • Escherichia coli Proteins
  • Oligodeoxyribonucleotides
  • Recombinant Proteins
  • Terpenes
  • Oxidoreductases
  • ispH protein, E coli
  • Mevalonic Acid

Associated data

  • GENBANK/AY062212