ENZYMES

Enzymes are macromolecular biological catalysts that accelerate chemical reactions. The
molecules upon which enzymes may act are called substrates, and the enzyme converts
the substrates into different molecules known as products.

Almost all metabolic processes in the cell need enzyme catalysis in order to occur at
rates fast enough to sustain life. Metabolic pathways depend upon enzymes to catalyze
individual steps.

The study of enzymes is called enzymology and a new field of pseudoenzyme analysis
has recently grown up, recognising that during evolution, some enzymes have lost the
ability to carry out biological catalysis, which is often reflected in their amino acid
sequences and unusual 'pseudocatalytic' properties.

Enzymes are known to catalyze more than 5,000 biochemical reaction types. Most
enzymes are proteins, although a few are catalytic RNA molecules. The latter are called
ribozymes. Enzymes' specificity comes from their unique three-dimensional structures.

Some enzymes are used commercially, for example, in the synthesis of antibiotics. Some
household products use enzymes to speed up chemical reactions: enzymes in biological
washing powders break down protein, starch or fat stains on clothes, and enzymes in
meat tenderizer break down proteins into smaller molecules, making the meat easier to
chew.

Like all catalysts, enzymes increase the reaction rate by lowering its activation energy.
Some enzymes can make their conversion of substrate to product occur many millions of
times faster. An extreme example is orotidine 5'-phosphate decarboxylase, which allows
a reaction that would otherwise take millions of years to occur in milliseconds.

Chemically, enzymes are like any catalyst and are not consumed in chemical reactions,
nor do they alter the equilibrium of a reaction. Enzymes differ from most other catalysts
by being much more specific. Enzyme activity can be affected by other molecules:
inhibitors are molecules that decrease enzyme activity, and activators are molecules that
increase activity.

Many therapeutic drugs and poisons are enzyme inhibitors. An enzyme's activity
decreases markedly outside its optimal temperature and pH, and many enzymes are
(permanently) denatured when exposed to excessive heat, losing their structure and
catalytic properties.
INTRODUCTION

The enormous variety of biochemical reactions that comprise life are nearly all mediated by a
series of remarkable biological catalysts known as enzymes. Although enzymes are subject to
the same laws of nature that govern the behavior of other substances,they differ from ordinary
chemical catalysts in several important respects:

1. Higher reaction rates:

The rates of enzymatically catalyzed reactions are typically factors of 106 to 1012 greater than
those of the corresponding uncatalyzed reactions and are at least several orders of magnitude
greater than those of the corresponding chemically catalyzed reactions.

2. Milder reaction conditions:

Enzymatically catalyzed reactions occur under relatively mild conditions:temperatures below
100°C, atmospheric pressure, and nearly neutral pH’s. In contrast, efficient chemical catalysis
often requires elevated temperatures and pressures as well as extremes of pH.

3. Greater reaction specificity:

Enzymes have a vastly greater degree of specificity with respect to the identities of both their
substrates(reactants) and their products than do chemical catalysts; that is, enzymatic reactions
rarely have side products. For example, in the enzymatic synthesis of proteins on ribosomes
,polypeptides consisting of well over 1000 amino acid residues are made all but error free. Yet,
in the chemical synthesis of polypeptides, side reactions and incomplete reactions presently
limit the lengths of polypeptides that can be accurately produced in reasonable yields to 200
residues

4. Capacity for control:

The catalytic activities of many enzymes vary in response to the concentrations of substances
other than their substrates and products.The mechanisms of these control processes include
allosteric control, covalent modification of enzymes, and variation of the amounts of enzymes
synthesized.
 CLASSIFICATION
(on the basis of reactions they catalyze)

Many enzymes have been named by adding the suffix “-ase” to the name of their substrate or to a
word or phrase describing their activity. Thus urease catalyzes hydrolysis of urea, and DNA
polymerase catalyzes the polymerization of nucleotides to form DNA. Other enzymes were
named by their discoverers for a broad function, before the specific reaction catalyzed was
known.

For example, an enzyme known to act in the digestion of foods was named pepsin, from the
Greek pepsis, “digestion,” and lysozyme was named for its ability to lyse (break down) bacterial
cell walls. Still others were named for their source: trypsin, named in part from the Greek tryein,
“to wear down,” was obtained by rubbing pancreatic tissue with glycerin.

Sometimes the same enzyme has two or more names, or two different enzymes have the same
name. Because of such ambiguities, and the ever-increasing number of newly discovered
enzymes, biochemists, by international agreement, have adopted a system for naming and
classifying enzymes.

This system divides enzymes into six classes, each with subclasses, based on the type of reaction
catalyzed . Each enzyme is assigned a four part classification number and a systematic name,
which identifies the reaction it catalyzes. As an example, the formal systematic name of the
enzyme catalyzing the reaction

ATP + D-glucose  ADP + D-glucose 6-phosphate

is ATP : glucose phosphotransferase, which indicates that it catalyzes the transfer of a

phosphoryl group from ATP to glucose.

Its Enzyme Commission number (E.C. number) is 2.7.1.1 The first number (2) denotes the class
name (transferase); the second number (7), the subclass (phosphotransferase); the third number
(1), a phosphotransferase with a hydroxyl group as acceptor; and the fourth number (1), D-
glucose as the phosphoryl group acceptor. For many enzymes, a trivial name is more frequently
used—in this case, hexokinase.

A complete list and description of the thousands of known enzymes is maintained by the
Nomenclature Committee of the International Union of Biochemistry and Molecular Biology.
International Classification of Enzyme

The top-level classification is:

 EC 1, Oxidoreductases: catalyze oxidation/reduction reactions

Transfer of electrons (hydride ions or H atoms)

 EC 2, Transferases: transfer a functional group (e.g. a methyl or phosphate group)

 EC 3, Hydrolases: catalyze the hydrolysis of various bonds

(transfer of functional groups to water)

 EC 4, Lyases: Cleavage of C—C, C—O, C—N, or other bonds by elimination,

leaving double bonds or rings, or addition of groups to double bonds

 EC 5, Isomerases: catalyze isomerization changes within a single molecule

 EC 6, Ligases: join two molecules with covalent bonds.