Affinities of various mammalian arachidonate lipoxygenases and cyclooxygenases for molecular oxygen as substrate

Biochim Biophys Acta. 1999 Jan 4;1436(3):509-18. doi: 10.1016/s0005-2760(98)00159-3.

Abstract

In an attempt to study affinities for molecular oxygen of mammalian arachidonate oxygenases, which remain unclarified at present, we determined activities of platelet-type 12-lipoxygenase, leukocyte-type 12-lipoxygenase, 5-lipoxygenase, 15-lipoxygenase, cyclooxygenase-1 and cyclooxygenase-2 at various oxygen concentrations. Activities of all the tested enzymes were assessed by oxygenation of radioactive arachidonic acid under hypoxic conditions, and part of the enzymes were also assayed by monitoring oxygen consumption. Their Km values for oxygen ranged between 10 and 26 microM. These results should be considered in investigations of arachidonic acid metabolism in pathophysiological processes associated with hypoxia.

Publication types

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

MeSH terms

  • Animals
  • Arachidonate 12-Lipoxygenase / metabolism
  • Arachidonate 15-Lipoxygenase / metabolism
  • Arachidonate 5-Lipoxygenase / metabolism
  • Arachidonate Lipoxygenases / metabolism*
  • Arachidonic Acid / metabolism
  • Blood Platelets / enzymology
  • Cyclooxygenase 1
  • Cyclooxygenase 2
  • Humans
  • Hypoxia / metabolism
  • In Vitro Techniques
  • Isoenzymes / metabolism
  • Kinetics
  • Leukocytes / enzymology
  • Membrane Proteins
  • Oxygen
  • Prostaglandin-Endoperoxide Synthases / metabolism*
  • Recombinant Proteins / metabolism
  • Substrate Specificity
  • Swine

Substances

  • Isoenzymes
  • Membrane Proteins
  • Recombinant Proteins
  • Arachidonic Acid
  • Arachidonate Lipoxygenases
  • Arachidonate 12-Lipoxygenase
  • Arachidonate 15-Lipoxygenase
  • Arachidonate 5-Lipoxygenase
  • Cyclooxygenase 1
  • Cyclooxygenase 2
  • PTGS1 protein, human
  • PTGS2 protein, human
  • Prostaglandin-Endoperoxide Synthases
  • Oxygen