my enzyme is cellulase. It has two domains( small domain and catalytic domain). small domain has a few hydrophobic interaction with catalytic domain. I determined PH optimum for truncated and wild-type enzyme( for truncated=7.5 and for wild-type= 6.5)
what causes Optimum PH become more basic ? can you give me a reason and article in order to rationalize this change?
I'll offer a speculation. Without the small domain, the environment of functional active site residues is less hydrophobic, which raises the pKa of one or more side chain (histidine or lysine), requiring a higher pH to deprotonate it, the deprotonated form being involved in catalysis.
Hi there
I suggest you reading the chapter 6th of the book Lehninger Principles of Biochemistry. I am sure you can find good explanations regarding the mechanism of enzyme activity. In short, as the pH changes, it surely means that the configuration of active site and the surrounding amino acids has changed in a way that resulted in the optimum pH increase.
Attached is the chapter 6 of the book.
Good luck
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