DESCRIBE THE CHEMISTRY OF TWO TYPES OF ENZYMES AND EXPLAIN HOW

THE APOENZYME FORMS

Enzymes can be defined as biological polymers that catalyze biochemical reactions.” Majority of
enzymes are proteins with catalytic capabilities crucial to perform different processes. Metabolic
processes and other chemical reactions in the cell are carried out by a set of enzymes that are
necessary to sustain life.  The initial stage of metabolic process depends upon the enzymes,
which react with a molecule and is called the substrate. Enzymes convert the substrates into other
distinct molecules and are called the products.  The regulation of enzymes has been a key
element in clinical diagnosis because of their role in maintaining life processes. The
macromolecular components of all enzymes consist of protein, except in the class of RNA
catalysts called ribozymes. The word ribozyme is derived from the ribonucleic acid enzyme.
Many ribozymes are molecules of ribonucleic acid, which catalyze reactions in one of their own
bonds or among other RNAs. Enzymes are found in all tissues and fluids of the body. Catalysis
of all reactions taking place in metabolic pathways is carried out by intracellular enzymes. The
enzymes in plasma membrane govern the catalysis in the cells as a response to cellular signals
and enzymes in the circulatory system regulate clotting of blood. Most of the critical life
processes are established on the functions of enzymes. Enzyme Structure Enzymes are a linear
chain of amino acids, which give rise to a three-dimensional structure. The sequence of amino
acids specifies the structure, which in turn identifies the catalytic activity of the enzyme. Upon
heating, enzyme’s structure denatures, resulting in a loss of enzyme activity, that typically is
associated with temperature.  Compared to its substrates, enzymes are typically large with
varying sizes, ranging from 62 amino acid residues to an average of 2500 residues found in fatty
acid synthase. Only a small section of the structure is involved in catalysis and is situated next to
the binding sites. The catalytic site and binding site together constitute the enzyme’s active site.
A small number of ribozymes exist which serve as an RNA-based biological catalyst. It reacts in
complex with proteins. Apo enzyme: The polypeptide or protein part of the enzyme is called the
Apo enzyme and may be inactive in its original synthesized structure. The inactive form of the
Apo enzyme 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 Apo enzyme. 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 Apo enzymes 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.

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REFERENCES

G. E. Schulz, R. H. Schemer: Principles of Protein Structure, Springer Verilog, New York 1990.

H. Gutfreund (ed.):Enzymes: 100 years.FEBS Letters, vol. 62, Suppl., North Holland, Amsterdam 1976

R. W. Old, S. B. Primrose: Principles of Gene Manipulation, Blackwell Scientific Publications, Oxford 1994