Change of product specificity of hexaprenyl diphosphate synthase from sulfolobus solfataricus by introducing mimetic mutations

Hisashi Hemmi, Motoyoshi Noike, Toru Nakayama, Tokuzo Nishino

Research output: Contribution to journalArticlepeer-review

6 Citations (Scopus)

Abstract

The introduction of several sets of amino acid substitutions into the region around a substrate-binding site of a medium-chain (all-E) prenyl diphosphate synthase, hexaprenyl diphosphate synthase from a thermoacidophilic archaeon Sulfolobus solfataricus, to mimic the product determination mechanisms of various kinds of short-chain enzymes revealed that the structure around the region of the medium-chain enzyme resembles those of eukaryotic farnesyl diphosphate synthases but not those of the other short-chain enzymes, reflecting the evolutional relationships among these enzymes.

Original languageEnglish
Pages (from-to)1096-1101
Number of pages6
JournalBiochemical and biophysical research communications
Volume297
Issue number5
DOIs
Publication statusPublished - 2002 Nov 6

Keywords

  • Archaeal enzyme
  • Chain-length determination
  • Evolution
  • Hexaprenyl diphosphate synthase
  • Isoprenoid
  • Mimetic mutation
  • Mutagenesis
  • Prenyl diphosphate synthase
  • Prenyltransferase
  • Terpenoid

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Fingerprint Dive into the research topics of 'Change of product specificity of hexaprenyl diphosphate synthase from sulfolobus solfataricus by introducing mimetic mutations'. Together they form a unique fingerprint.

Cite this