Question

why mostly enzymes are found in tertiary or 3 degree tructure. give reaons.

Answer 1

sorry its structure not tructure

Answer 2

I don't understand the question because most* proteins, not just enzymes, have well defined tertiary or overall structure. All I can think of are globular proteins - like protein kinases - with discrete, well formed domains which move in relation to the enzyme's status as it interacts with its substrate, product, regulatory molecules, post translational modifications and general ionic environment in which it's placed.

Provide a more detailed, better worded question and I'll give you a more detailed, better worded answer, please.

* Some proteins, especially signal transduction and transcription related proteins, are 'disordered' - that is, they have regions of highly variable and plastic structure. Enzymes tend to be highly structured because their inactive states must recognize and bind specifically to a certain specific substrate and often to regulatory molecules and proteins as well. Enzymatic catalysis is often accompanied by large changes in tertiary or overall protein structure, as is enzymatic regulation in which noncompetitive inhibitors interact with the protein and affect its overall structure in such a way that substrates can no longer bind to it.

Answer 3

Actually a noncompetitive inhibitor doesnt bind to the active site of the enzyme but substrates are still able to bind to the active site but at a lower affinity to the active site due to the conformational change by the allosteric inhibitor. It will have a lower Vmax [reactions of Substrate to products per unit of time]

Proteins are usually in tertiary structure or higher due to the folding of the primary structure that gives its shape. It is also in its equilibrium state [favorable conformation under physiological conditions]