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PMID: 5801304 Published · ppublish English Journal Article

Competition of two substrates for a single enzyme. A simple kinetic theorem exemplified by a hydroxy steroid dehydrogenase reaction.

The Biochemical journal ·Vol. 112 ·No. 3 ·1969-04-00 ·Pages 331-4

Pocklington T, Jeffery J

Abstract

1. If two compounds are substrates for a single enzyme, and do not form any ternary complex with the enzyme or combine directly with each other, then the total initial rate of reaction for a mixture of the two compounds may be greater than the rate for either compound alone, or may lie between the rates for the compounds alone. It is the concentration of the compound with the higher maximum velocity that determines which applies, and there is one concentration of the compound of higher maximum velocity at which the total rate of reaction is independent of the presence or absence of the substrate of lower maximum velocity. The values concerned are derived. 2. An example is given of 5alpha-androstan-3-one and 5alpha-androstane-3,16-dione as substrates competing for a hydroxy steroid-NAD oxidoreductase (EC 1.1.1.53).

MeSH Terms
Androstanes Chemical Phenomena Chemistry Hydroxysteroid Dehydrogenases/antagonists & inhibitors Kinetics
Chemicals
Androstanes Hydroxysteroid Dehydrogenases
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Pocklington T
Jeffery J
References (3)
3 references, click to expand
  1. 3 alpha-hydroxysteroid: NAD oxidoreductase activity in crystalline preparations of 20 beta-hydroxysteroid: NAD oxidoreductase.
    Eur J Biochem. 1968 Dec;7(1):63-7 PMID: 4303403
  2. Lactic dehydrogenase. II. Variation of kinetic and equilibrium constants with temperature.
    J Biol Chem. 1956 Jul;221(1):191-209 PMID: 13345810
  3. [20 beta-Hydroxysteroid dehydrogenase, a new crystalline enzyme].
    Biochim Biophys Acta. 1959 Sep;35:270-2 PMID: 14403760
Article Info
Journal
The Biochemical journal
Abbr.
Biochem J
ISSN
0264-6021
Published
1969-04-00
Pages
331-4
Language
English
Region
England
NLM ID
2984726R
PMCID
PMC1187712
Subset
IM
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