The Transient-State Kinetics of Two-Substrate Enzyme Systems Operating by an Ordered Ternary-Complex Mechanism
Author:
Publisher
Wiley
Subject
Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1432-1033.1976.tb10883.x/fullpdf
Reference13 articles.
1. Transient-Phase and Steady-State Kinetics for Enzyme Systems Involving Two Substrates
2. Influence of premixing on transient-phase kinetics for two-substrate enzyme systems
3. Mechanistic studies on equine liver alcohol dehydrogenase. I. Stoichiometry relation of the coenzyme binding sites to the catalytic sites active in the reduction of aromatic aldehydes in the transient state
4. Catalytic steps during the single-turnover reduction of aldehydes by alcohol dehydrogenase
5. Mechanistic studies on horse liver alcohol dehydrogenase. Influence of the different premixings on the transient kinetics of aldehyde reductions
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