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Bookmark or Share- Why does uncompetitive inhibition decrease the Michaelis constant?I can't seem to find a good resource online that clearly outlines the difference between an uncompetitive, noncompetitive, and mixed inhibitor (I understand competitive inhibitor though). More
- Enzyme kinetics: Effect of immobilization on kinetic parameterskcat 0.5 1/min Km 0.6 microM [E0] 5 micro M [S] 60 micro M Could I expect to retain them after immobilization? Or are these too high for an immobilized enzyme? If it matters, it is a 500 residue enzyme with a MW of approx. 65,000 Da
- kcat in uncompetitive enzyme inhibition - Biology Stack ExchangeAside from grammar and punctuation fixes, your question needs attention to the following issues: 1. Please mention the source of the information (kcat remaining unchanged in uncompetitive inhibition) and the context in which it was given. 2. 'enzyme–substrate work efficiency' is not a well defined term in biology. Can you word it better?
- What is the meaning behind Kcat / Km? - Biology Stack Exchange$\begingroup$ "There is an upper limit to Kcat / Km, imposed by the rate at which E and S can diffuse together in an aqueous solution. This diffusion controlled limit is 10^8 to 10^9 , enzymes with a Kcat / Km near this range are said to have achieved catalytic perfection"(Lehninger) This would be a strange assumption if the value "doesn't ...
- Does pH affect Michaelis constant? - Biology Stack Exchange$\begingroup$ @wswr kr is dissociation rate constant. kcat is the turnover number or the rate constant of product formation. Both these reduce the concentration of the [ES] complex. $\endgroup$ – WYSIWYG
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