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 const
โฆ LIBER โฆ
Multiple steady-state phenomena within enzyme reactors: The enzyme reaction with two substrates
โ Scribed by Ian A. Webster; Michael L. Shuler
- Publisher
- John Wiley and Sons
- Year
- 1981
- Tongue
- English
- Weight
- 643 KB
- Volume
- 23
- Category
- Article
- ISSN
- 0006-3592
No coin nor oath required. For personal study only.
๐ SIMILAR VOLUMES
Steady state kinetics of enzymes with su
โ
Eric A. Barnsley
๐
Article
๐
1990
๐
Elsevier Science
๐
English
โ 190 KB
Simple and direct derivation of steady-s
โ
Ivan G. Darvey
๐
Article
๐
1996
๐
Elsevier Science
๐
English
โ 292 KB
Steady state multiplicity of adiabatic g
โ
Shanmuk Sharma; Lee A. Hoffman; Dan Luss
๐
Article
๐
1976
๐
American Institute of Chemical Engineers
๐
English
โ 801 KB
The relationship between steady-state ki
โ
I.G. Darvey
๐
Article
๐
1973
๐
Elsevier Science
๐
English
โ 436 KB
Steady state kinetics of consecutive enz
โ
P.W. Kuchel; L.W. Nichol; P.D. Jeffrey
๐
Article
๐
1974
๐
Elsevier Science
๐
English
โ 695 KB
One-substrate-one-product enzymic reacti
โ
I.G. Darvey
๐
Article
๐
1975
๐
Elsevier Science
๐
English
โ 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