Explain the effect of PH on ezymes activity ? I need this for my homework.
2007-11-19 01:45:13 · 4 answers · asked by LIZA 4 in Science & Mathematics ➔ Chemistry
Some amino acids, aspartic and glutamic acids, have -COOH side chains. Others, lysine, arginine, tryptophan, histidine, have >NH side chains. At low pH's, >NH + H+ ===> >NH2+. At high pH's, -COOH + OH- ===> -COO(-) + H2O. These charges on amino acid side chains could attract or repel one another, altering the folding of the protein. Altered folding could destroy or decrease enzymatic activity.
2007-11-19 01:51:58 · answer #1 · answered by steve_geo1 7 · 2⤊ 0⤋
Enzymes paintings by potential of allowing reactions to take place. contained regarding the lysozome, breaking down an Hydrogen atom is donated by potential of a Glutamate area chain. bear in mind that there is a particular energetic internet site for catalysis. Glu35 ought to have an H available to donate to start the reaction. In a intense PH atmosphere, the H has been stripped away, and this prevents the reaction
2016-11-12 02:11:23 · answer #2 · answered by ? 4 · 0⤊ 0⤋
Different enzymes have different optimum pH values that they work most efficeintly at. The concentration of H+ ions affects the hydrogen bonds holding the amino acid chain (primary structure) in its specific arrangement (secondary and tertiary structure) . This can alter the shape of the active site where the enzymic reaction takes place.
2007-11-19 01:51:13 · answer #3 · answered by freakyjouk 1 · 1⤊ 0⤋
Enzymes work best in alkaline conditions. This is done and maintained by the bile that is produced by the liver and stored in the gall bladder.
2007-11-19 01:52:39 · answer #4 · answered by Anonymous · 0⤊ 1⤋