Protein Biocatalyst (Enzyme)

Role of Enzymes in Biochemical Reactions An enzyme is a protein molecule that is a biological catalyst with three characteristics. First, the basic function of an enzyme is to increase the rate of a reaction. Most cellular reactions occur about a million times faster than they would in the absence of an enzyme. Second, most enzymes act specifically with only one reactant (called a substrate) to produce products. The third and most remarkable characteristic is that enzymes are regulated from a state of low activity to high activity and vice versa. Much of the information about enzymes has been made possible because they can be isolated from cells and made to work in a test tube environment. Extensive work has also been done with X-Ray diffraction techniques to elucidate the three-dimensional structure of some enzymes. Enzyme Parts List The activity of an enzyme depends, at the minimum, on a specific protein chain. In many cases, the enzyme consists of the protein and a combination of one or more parts called cofactors. This enzyme complex is usually simply referred to simply as the enzyme. Apoenzyme: The polypeptide or protein part of the enzyme is called the apoenzyme and may be inactive in its original synthesized structure. The inactive form of the apoenzyme is known as a proenzyme or zymogen. The proenzyme may contain several extra amino acids in the protein which are removed, and allows the final specific tertiary structure to be formed before it is activated as an apoenzyme. Cofactors: A cofactor is a non-protein substance which may be organic, and called a coenzyme. The coenzyme is often derived from a vitamin with specific examples discussed later. Another type of cofactor is an inorganic metal ion called a metal ion activator. The inorganic metal ions may be bonded through coordinate covalent bonds. The major reason for the nutritional requirement for minerals is to supply such metal ions as Zn+2, Mg+2, Mn+2, Fe+2, Cu+2, K+1, and Na+1 for use in enzymes as cofactors. Final Enzyme: The type of association between the cofactor and the apoenzymes varies. In some cases, the bonds are rather loose and both come together only during the course of a reaction. In other cases, they are firmly bound together by covalent bonds. The activating role of a cofactor is to either: activate the protein by changing its geometric shape, or by actually participating in the overall reaction. The overall enzyme contains a specific geometric shape called the active site where the reaction takes place. The molecule acted upon is called the substrate.

The latest systematic nomenclature system known as the International Enzyme Commission (IEC) system is based upon the type of reaction catalyzed. There are six broad groups of enzymes in this system as shown: Oxidoreductases Enzymes responsible for oxidation either by the addition of oxygen or removal of hydrogen or electrons are called oxidases. On the contrary, the enzymes which add hydrogen or electrons are termed as reductases. Most of the enzymes which bring about oxidation or reduction perform the reaction simultaneously, ex. Cytochrome oxidase, nitrate reductase, a-ketoglutamate dehydrogenase. Transferases Certain groups like amino groups, acyl groups, phosphates can be transferred from one compound to another compound by specific transferase enzymes, ex. Aminotransferases, transcarboxylases, transhydrogenases, transacetylases. Hydrolases The enzymes which by adding water molecules bring about breakdown of bonds are called hydrolases. Majority of lysosomal enzymes are hydrolases of one or the other kind, ex. Lipases, proteases, DNase, RNAase, Amylase, endonuclease. Lyases These enzymes add a group to compounds containing double bonds between carbon and carbon, carbon and nitrogen, carbon and oxygen.

Isomerases Enzymes which are capable of transforming one isomer to another are called isomerases. They are highly specific in their substrates and reactions, ex. Glucose 6-p isomerase converts glucose 6-p to fructose6p. Phosphoglyceraldehyde can be converted to another isomer called dihydroxyacetone phosphate by gluoco-phospho glyceraldehyde isomerase. Ligases Ligase enzymes bring about the bond formation between different molecules by removing a molecule of water. In fact, their activities is in the opposite direction of hydrolyses. They bring about the synthesis of bigger compounds by the addition of simpler compounds. Such enzymes are also called synthetases. ex. RNA polymerases, DNA polymerase, peptidyl transferase.