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By G. W. Stout, N. P. O. Green (auth.)

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An enzyme-cofactor complex is called a holoenzyme. An enzyme without its cofactor is called an apoenzyme. g. salivary amylase activity is increased by the presence of chloride ions. g. FAD, haem. g. NAD,ATP. Prosthetic groups and coenzymes act as carriers of groups of atoms. c Enzyme Inhibition A number of small molecules can reduce the rate of an enzyme-controlled reaction: 1 Competitive reversible inhibition: a compound similar in structure to the usual enzyme substrate competes for a place on the enzyme's active site.

This causes a change in the molecular configuration of the active site and affects its ability to form a substrate-enzyme complex. The net effect is a reduction in catalytic activity. Extreme changes in pH alter the ionic charges on acidic and basic groups of peptide chains in the enzyme molecule. They can also destroy the secondary and tertiary protein structures by breaking hydrogen bonds and disulphide bridges. c reaction rate satu ration of active sites substrate concentration For a given enzyme concentration the rate of an enzyme-mediated reaction increases with increasing substrate concentration in a linear fashion.

The former, collectively called the light reaction, involves light energy, absorbed by chlorophylls and carotenoids. This light energy 'splits' water molecules (photolysis) into hydrogen and oxygen. The latter is released as gaseous oxygen. In the non-light-dependent reactions, or dark reactions, hydrogen combines with (reduces) carbon dioxide to form carbohydrate. The overall equation can be represented as shown below.

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