Could some one provide me with some resources or papers where I can read more about the following:
1- How can the 3D structure of an enzyme affect its Km and Vmax? (some papers, books or articles will be very neat).
2- How can the solubility of the amino acids of the binding site of an enzyme affect its Km and Vmax? (again some paper, books or articles will be very helpful).
Or maybe some description about that with some references? I spent some time in searching but unfortunately with no attractive results.
Thanks in advance!
Most anything that effects the binding of substrate or the release of product will affect the enzyme constants, and this to an uncertain degree, with the most likely being non-competitive inhibition. I don't think that there is a computational way to figure this out and it must be done experimentally. Graph your experiments using a Lineweaver-Burk plot. These plots can be used to determine competitive (a different substrate), irreversible (cannot convert to product or binding irreversibly), and noncompetitive inhibition (destabilizes the protein or active site, or by binding somewhere on it - not the active site). I believe you would have to engineer and express the changes in the enzyme and then measure. Good luck!!
https://en.wikipedia.org/wiki/Lineweaver%E2%80%93Burk_plot
Dear Mohammed:
I suggest you to have a loof to the book " Lehninger: Principles of Biochemistry". You will find the answer for all your questions.
Best wishes,
Rosa María
The proteins behave differently in this regard. We cannot draw a conclusion about one enzyme because another enzyme's structure is related in some way to its Vmax or Km.
The contribution of the 3D structure to these values cannot be "quantified" in a meaningful way.
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