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In chemistry, the term "turnover number" has two distinct meanings.. In enzymology, the turnover number (k cat) is defined as the limiting number of chemical conversions of substrate molecules per second that a single active site will execute for a given enzyme concentration [E T] for enzymes with two or more active sites. [1]
To address such a paradox, Kuo-Chen Chou and his co-workers proposed a model by taking into account the spatial factor and force field factor between the enzyme and its substrate and found that the upper limit could reach 10 10 M −1 s −1, [6] [7] [8] and can be used to explain some surprisingly high reaction rates in molecular biology. [5 ...
, which is often written as , [5] represents the limiting rate approached by the system at saturating substrate concentration for a given enzyme concentration. The Michaelis constant K m {\displaystyle K_{\mathrm {m} }} is defined as the concentration of substrate at which the reaction rate is half of V {\displaystyle V} . [ 6 ]
Enzyme kinetics: behavior and analysis of rapid equilibrium and steady state enzyme systems. New York: Wiley. ISBN 978-0-471-30309-1. Advanced. Fersht A (1999). Structure and mechanism in protein science: a guide to enzyme catalysis and protein folding. San Francisco: W.H. Freeman. ISBN 978-0-7167-3268-6. Schnell S, Maini PK (2004).
The reaction catalyzed by CA1 is the same as other carbonic anhydrase family proteins: + (in tissues - high CO 2 concentration) [9]. The CA1-catalyzed reaction has a relatively low reaction affinity (Km) of 4.0 mM for CO 2, [7] [10] turnover number (Kcat) of 2 × 10 5 s −1, and catalytic efficiency (Kcat/Km) of 5 × 10 7 M −1 s −1 comparing to other isozymes of the α-CA family of ...
An anhydrase is defined as an enzyme that catalyzes the removal of a water molecule from a compound, and so it is this "reverse" reaction that gives carbonic anhydrase its name, because it removes a water molecule from carbonic acid. In the lungs carbonic anhydrase converts bicarbonate to carbon dioxide, suited for exhalation.
An active site titration process can be done for the elimination of errors arising from differences in cultivation batches and/or misfolded enzyme and similar issues. This is a measure of the amount of active enzyme, calculated by e.g. titrating the amount of active sites present by employing an irreversible inhibitor.
This page was last edited on 3 July 2015, at 02:10 (UTC).; Text is available under the Creative Commons Attribution-ShareAlike 4.0 License; additional terms may apply ...
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