Are there other ways, besides heat, of controlling enzymatic activity? Give an example.

Question

Julian Aguilar · Accepted Answer

Changing pH, the presence of co-factors, the choice of buffer, and the availability of substrates can all influence enzymatic activity.

1. pH To begin with, pH is crucial; adjusting it will affect the rate of reaction. However, you must exercise caution because even a tiny deviation can have disastrous (and typically irreversible) consequences. 2: Co-Factors A lot of enzymes are inactive by themselves, and need to be "started up" by a co-factor, or co-Enzyme. This can be a simple ion (#Ca^"++"# and #Mg^"++"# are well-known ones), but also a more complicated molecule (e.g. Co-enzymeA). 3: Buffer Although most common enzymes are quite content with standard TRIS/TBE Buffers, the choice of buffer can still have an impact (depends on the specific enzyme) 4: "Strangling" Reaction rate will be impacted by decreasing the quantity (read: availability) of any substrate that an enzyme uses, but only in a negative way.

Penelope Adams · Answer

undefined Yes, pH levels can also control enzymatic activity. An example is pepsin, which functions optimally in the acidic environment of the stomach.