Respuesta :
Answer:
During gluconeogenesis and glycolysis, Enolase catalyzes the transformation of 2-phosphoglycerate to phosphoenolpyruvate and is needed by every domain of life.
Explanation:
The optimum pH required is 6.5. Changes in pH value affect both hydrogen and ionic which hold the enzymes together. The changes may not only alter the enzyme's structure, but may also modify the substratum's form or charging properties so that either the substratum can't bind to the active site or catalyze it.
Like other enzymes, enolase is influenced by environmental factors. pH is one of these factors. Changes in pH affect enymatic structure and function.
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Enzymes, like all proteins, are polypeptidic molecules. They need to get an accurate tridimensional structure to accomplish their function.
There is a limited temperature and pH level at which they lose that structure and denaturalize.
- pH changes
The most accurate configuration for the best catalytic performance depends on the charge of the lateral chains and the environmental pH.
Enzymes have ionizable chemical groups in the lateral chains of their amino acids.
Depending on the environmental pH, these groups will have a positive, negative, or neutral charge.
There is an optimum pH level at which enzymes get the best configuration to accomplish their functions.
Regarding the enzymatic rate of reaction,
- below the optimum pH level, the enzyme has not reached its maximum activity level yet,
- at higher pH levels, the rate of reaction decreases notoriously, which is related to its structure.
Most enzymes are sensitive to any change in pH, which might drastically affect their activity. So every enzyme has its optimum pH level, and any slight deviations will cause the enzyme denaturalization, hence, its activity loss.
ENOLASE
Enolase is an enzyme involved in glycolysis, expressing an optimum pH level between 6.5 and 8.0.
This molecule is found in all tissues and organisms capable of producing fermentation or glycolysis.
Enolase is composed of three subunits. They might combine in different ways producing five possible isoenzymes depending on the combination.
Each subunit is composed of an alfa helix and beta-sheet, and the molecule gets a compact and globular structure.
Changes in pH might
- affect bonds between these subunits, altering the whole globular structure of the protein.
- alter ionization of the substrate
- influence the binding of the substrate to the enzyme and its reactivity in catalysis.
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