Six Types of Enzyme Catalysts

Although a huge number of reactions occur in living systems, these reactions fall into only half a dozen types. The reactions are: 1. Oxidation and reduction. Enzymes that carry out these reactions are calledoxidoreductases. For example, alcohol dehydrogenase converts primary alcohols to aldehydes.

In this reaction, ethanol is converted to acetaldehyde, and the cofactor, NAD, is converted to NADH. In other words, ethanol is oxidized, and NAD is reduced. (The charges don't balance, because NAD has some other charged groups.) Remember that in redox reactions, one substrate is oxidized and one is reduced. 2. Group transfer reactions. These enzymes, called transferases, move functional groups from one molecule to another. For example, alanine aminotransferase shuffles the alpha-amino group between alanine and aspartate:

3. Other transferases move phosphate groups between ATP and other compounds, sugar residues to form disaccharides, and so on. 4. Hydrolysis. These enzymes, termed hydrolases, break single bonds by adding the elements of water. For example, phosphatases break the oxygen-phosphorus bond of phosphate esters:

5. Other hydrolases function as digestive enzymes, for example, by breaking the peptide bonds in proteins. 6. Formation or removal of a double bond with group transfer. The functional groups transferred by these lyase enzymes include amino groups, water, and ammonia. For example, decarboxylases remove CO2 from alpha- or beta-keto acids: Dehydratases remove water, as in fumarase (fumarate hydratase):

Deaminases remove ammonia, for example, in the removal of amino groups from amino acids:

7. Isomerization of functional groups. In many biochemical reactions, the position of a functional group is changed within a molecule, but the molecule itself contains the same number and kind of atoms that it did in the beginning. In other words, the substrate and product of the reaction are isomers. Theisomerases (for example, triose phosphate isomerase, shown following), carry out these rearrangements.

8. Single bond formation by eliminating the elements of water. Hydrolases break bonds by adding the elements of water; ligases carry out the converse reaction, removing the elements of water from two functional groups to form a single bond. Synthetases are a subclass of ligases that use the hydrolysis of ATP

to drive this formation. For example, aminoacyl-transfer RNA synthetasesjoin amino acids to their respective transfer RNAs in preparation for protein synthesis; the action of glycyl-tRNA synthetase is illustrated in this figure:

Carboxypeptidase A

Carboxypeptidase A is a digestive enzyme that hydrolyzes the carboxyl-terminal peptide bond in polypeptide chains.

Hydrolysis occurs most readily if the carboxyl-terminal residue has an aromatic or a bulky aliphatic side chain. (Stryer,1988) The enzyme serves as a good illustration of protein secondary structure. The single polypeptide chain of 307 amino acids contains regions of alpha helix (385) and beta pleated sheet (17%). Carboxypeptidase A also demonstrates two important catalytic mechanisms :

induced fit electronic strain

Binding of a typical substrate such as glycyl-tyrosine results in a structural rearrangement of the active site (induced fit). Residues which are thought to interact with the substrate include Glutamate 270, Arginine 145, Arginine 127, and Tyrosine 248. A zinc atom is coordinated in a tetrahedral array with the amino acids Histidine 69, Histidine 196, and Glutamate 72, and either a water or substate molecule. The zinc atom is a prosthetic group that is essential for enzymatic activity and is largely responsible for the electronic strain created at the active site. In the illustration below, zinc polarizes the carbonyl group of the peptide bond in glycyl-tyrosine, making it more susceptible to attack by Glutamate 270.

(Stryer,1988)