Structure of active IspH enzyme from Escherichia coli provides mechanistic insights into substrate reduction

Angew Chem Int Ed Engl. 2009;48(31):5756-9. doi: 10.1002/anie.200900548.
No abstract available

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Biocatalysis
  • Catalytic Domain
  • Electron Transport
  • Escherichia coli / enzymology*
  • Escherichia coli Proteins / chemistry*
  • Escherichia coli Proteins / metabolism
  • Hemiterpenes / biosynthesis
  • Hemiterpenes / chemistry
  • Organophosphorus Compounds / chemistry
  • Oxidoreductases / chemistry*
  • Oxidoreductases / metabolism
  • Protein Structure, Tertiary
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / metabolism

Substances

  • Escherichia coli Proteins
  • Hemiterpenes
  • Organophosphorus Compounds
  • Recombinant Proteins
  • isopentenyl pyrophosphate
  • 3,3-dimethylallyl pyrophosphate
  • Oxidoreductases
  • ispH protein, E coli