We all know that the active site of an enzyme consists of Catalytic site and Substrate binding site. So, my question is, does the enzyme still have catalytic activity after the enzyme's substrate binding domain is removed? ths
In my opinion, no activity. However, after the substrate binding domain of κ-carrageenase was deleted, the remaining part still have activity to κ-carrageenan, and almost same to the original one. a bit strange...
It is quite common for enzymes degrading large carbohydrate polymers to possess a substrate-binding domain that is distinct from the catalytic domain. Removal of the substrate-binding domain will generally impair the activity toward insoluble and particulaly crystalline substrates (e.g. in the case of cellulases), but activity against soluble or amorphous substrates is usually conserved
Depends on what the residual substrate affinity of the catalytic domain is - you would definitely expect a much higher Michaelis-Menthen Constant.
Exactly, thank you very much, I also gone through some pubulished articles, and got the same answer. @Pierre Béguin, Annemarie Honegger thanks again.
No, as Enzyme are specific because of active site in which there are specific amino acids resides which help in substrate binding.
To Abhishek Sharma : thanks for ur answer. however, i think Pierre Béguin's answer is exactly right.
According to induced fit theory of mechanism of enzyme catalysis loss of substrate binding site may lead to loss of catalytic activity to maximum extant. Because precise catalytic site forms only after substrate binding .
In case of allosteric enzymes where effector molecules bind site other than substrate binding site catalytic activity may not be affected.
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