Decaprenyl pyrophosphate synthetase from Paracoccus denitrificans

Koichi Ishii, Hiroshi Sagami, Kyozo Ogura

Research output: Contribution to journalArticlepeer-review

12 Citations (Scopus)

Abstract

Decaprenyl pyrophosphate synthetase was partially purified from extracts of Paracoccus denitrificans. The enzyme catalyzed the synthesis of all-E-decaprenyl pyrophosphate from isopentenyl pyrophosphate and geranyl pyrophosphate, but it did not catalyze a reaction between isopentenyl pyrophosphate and dimethylallyl pyrophosphate. The Michaelis constants for geranyl, E,E-farnesyl pyrophosphate, and al-E-geranyl-geranyl pyrophosphate were 5.0 0.06, and 2.9 μM, respectively. The enzyme required detergent and Mg2+ for its catalytic activity and it was activated by monovalent cations such as K+ and NH4+.

Original languageEnglish
Pages (from-to)291-297
Number of pages7
JournalBiochimica et Biophysica Acta (BBA)/Lipids and Lipid Metabolism
Volume835
Issue number2
DOIs
Publication statusPublished - 1985 Jul 9

Keywords

  • (P. denitrificans)
  • Decaprenyl pyrophosphate synthetase
  • Prenyltransferase

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Endocrinology

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