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Steady state kinetics of enzymes with substrates having multiple reaction sites

โœ Scribed by Eric A. Barnsley

Publisher
Elsevier Science
Year
1990
Tongue
English
Weight
190 KB
Volume
142
Category
Article
ISSN
0022-5193

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โœฆ Synopsis

An enzyme catalysing the reaction of a substrate with multiple reaction sites may display steady state kinetics described by a Michaels-Menten equation. The K m is identical for all sites considered individually and all sites together. The maximum velocity for a single site depends on the rate constants for reaction at that site and at all of other sites.

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โœ I.G. Darvey ๐Ÿ“‚ Article ๐Ÿ“… 1975 ๐Ÿ› Elsevier Science ๐ŸŒ English โš– 464 KB

Expressions are derived for the parameters that can be obtained from (1) steady-state kinetics, (2) isotope-exchange kinetics at equilibrium, and (3) equilibrium binding experiments for the following two one-substrateone-product enzymic mechanisms: It is shown that the exchange constants for both m