In most cases, it is noted that copper complexes exhibited excellent enzyme inhibition activities. But I have got a reverse result which means copper complex has got lower inhibition on amylase. Please suggest any relevant chemistry for this result
Dear Anjali Krishna G sorry to see that your very interesting technical question has not yet received any expert answers. We work in the field of organometallic chemistry, so that I'm not really a specialist in this area of research. However, I made the experience that it often pays off to directly use RG as a valuable source of information. Many relevant research articles have been posted by RG members, some of them even as public full texts. For example, please have a look at the following potentially useful paper which is freely accessible on RG:
REVIEW: Metal complexes as urease inhibitors
Article REVIEW: Metal complexes as urease inhibitors
I hope this helps. Good luck with your work and best wishes!
Copper, zinc, and nickel complexes with the same ligand will almost always have different structure (and stability). Thus, one such complex can fit better to the enzyme than the other and this can change the inhibition efficiency.
To answer your question in more detail, we would need to know the structure of the ligand forming the complex.