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Biochemistry (Moscow)

, Volume 72, Issue 9, pp 944–953 | Cite as

Molecular oxygen (a substrate of the cyclooxygenase reaction) in the kinetic mechanism of the bifunctional enzyme prostaglandin-H-synthase

  • I. S. Filimonov
  • P. V. Vrzheshch
Article

Abstract

Prostaglandin-H-synthase is a bifunctional enzyme catalyzing conversion of arachidonic acid into prostaglandin H2 as a result of cyclooxygenase and peroxidase reactions. The dependence of the rate of the cyclooxygenase reaction on oxygen concentration in the absence and in the presence of electron donor was determined. A two-dimensional kinetic scheme accounting for independent proceeding and mutual influence of the cyclooxygenase and peroxidase reactions and also for hierarchy of the rates of these reactions was used as a model. In the context of this model, it was shown that there are irreversible stages in the mechanism of the cyclooxygenase reaction between points of substrate donation (between donation of arachidonic acid and the first oxygen molecule and also between donation of two oxygen molecules).

Key words

prostaglandin-H-synthase bifunctional enzyme cyclooxygenase activity kinetic mechanism oxygen arachidonic acid adrenaline 

Abbreviations

AA

arachidonic acid

D

oxidized form of electron donor

DH

reduced form of electron donor

PGG2

prostaglandin G2

PGH2

prostaglandin H2

PGHS

prostaglandin-H-synthase

PP

protoporphyrin IX

ROOH

peroxide

Tyr

tyrosine residue

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Copyright information

© Pleiades Publishing, Ltd. 2007

Authors and Affiliations

  1. 1.Faculty of Bioengineering and BioinformaticsLomonosov Moscow State UniversityMoscowRussia
  2. 2.Emanuel Institute of Biochemical PhysicsRussian Academy of SciencesMoscowRussia
  3. 3.International Biotechnological CenterLomonosov Moscow State UniversityMoscowRussia

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