Biochemistry Assignment

Topic: Enzymes
Date: 9th, May, 2013
Submitted by Najwa Nadeem, Roll #113, Batch B, 1st year M.B.B.S.

Classification of Enzymes
The main classes of enzymes are as follows:

Class 1: Oxidoreductases
Oxidoreductases catalyze oxidation reduction reactions. At least one substrate becomes
oxidized and at least one substrate becomes reduced. This group of enzymes usually
utilizes NADP or NAD+ as cofactors. They further consist of 4 classes-oxidases,
dehydrogenases, hydroperoxidases and oxygenases.
Class 2: Transferases
Transferases catalyze group transfer reactions- the transfer of a functional group from one
molecule to another. There various subtypes include aminotransferases,
phosphotransferases, methyl transferases, acyl transferases and so on.
Class 3: Hydrolases
In hydrolysis reactions, C-O, C-N, and C-S bonds are cleaved by addition of HO in the
form of OH- and H+ to the atoms forming the bond. Large compounds are hydrolysed to
smaller ones by the addition of water. An example is digestive enzymes of carbohydrates,
proteins, lipids, DNA and RNA.
Class 4: Lyases
Lyases cleave C-C, C-O, C-N, and C-S bonds by means other than hydrolysis or
oxidation. They either incorporate double bonds or they saturate existing double binds.

Class 5: Isomerases
Isomerases just rearrange the existing atoms of a molecule, that is, create isomers of the
starting material.
Class 6: Ligases
Ligases synthesize C-C, C-S, C-O, and C-N bonds in reactions coupled to the cleavage of
high energy phosphate bonds in ATP or some other nucleotide.

Enzyme Terminology
The first Enzyme Commission, in its report in 1961, devised a system for classification of
enzymes that also serves as a basis for assigning code numbers to them. These code numbers,
prefixed by EC, which are now widely in use, contain four elements separated by points, with the
following meaning:
1.
2.
3.
4.

The first number shows to which of the six main divisions (classes) the enzyme belongs,
The second figure indicates the subclass,
The third figure gives the sub-subclass,
The fourth figure is the serial number of the enzyme in its sub-subclass.

For example EC 1.1.1.1 shows alcohol dehydrogenase of class 1 enzymes.

Properties of Enzymes
Enzymes are large biological molecules responsible for the thousands of chemical
interconversions that sustain life. They are highly selective catalysts, greatly accelerating both
the rate and specificity of metabolic reactions, from the digestion of food to the synthesis of
DNA. Most enzymes are proteins, although some catalytic RNA molecules have been identified.
Enzymes adopt a specific three-dimensional structure, and may employ organic (e.g. biotin) and
inorganic (e.g. magnesium ion) cofactors to assist in catalysis.

Being proteins in nature, enzymes are produced by transcription and translation and can
be regulated at any level (e.g. post-translational modification). They have a specific 3dimensional structure which can be damaged in unfavourable conditions. They require
optimum temperature and pH for maximum activity. Otherwise they may be permanently
or reversibly denatured.
Some enzymes are secreted as proenzymes (zymogens). These are inactive enzyme
precursors. The pancreas secretes zymogens partly to prevent the enzymes from digesting
proteins in the cells in which they are synthesised. Enzymes like pepsin are created in the
form of pepsinogen, an inactive zymogen. Pepsinogen is activated when Chief cells
release it into HCl which partially activates it. Another partially activated pepsinogen
completes the activation by removing the peptide turning the pepsinogen into pepsin.
Accidental activation of zymogens can happen when the secretion duct in the pancreas is
blocked by a gallstone resulting in acute pancreatitis.

Enzymes are usually very specific as to which reactions they catalyze and the substrates
that are involved in these reactions. Complementary shape, charge and
hydrophilic/hydrophobic characteristics of enzymes and substrates are responsible for
this specificity. Enzymes specific for one substrate only show absolute specificity while
those specific for particular group show relative specificity. For example hexokinase
enzymes act on hexoses but not pentoses.
Enzymes catalyzing reversible reactions follow the law of mass action.
Substrate

Product

For example Glucose-6-phosphate

Fructose-6-phosphate
The enzyme used is phosphor-glucose-isomerase.
When glucose-6-phosphate is in large concentration in glycolysis, the reaction moves in
the forward direction. In gluconeogenesis, glycolysis is almost stopped (in fasting
conditions) and the reaction goes backward as fructose-6-phosphate is now in high
concentration.
Enzyme induction is a process in which a molecule induces the expression of an enzyme
in response to some stimulus. 90% stimulation is at the level of transcription.
Glucokinase is an enzyme produced in the liver and induced by insulin. As insulin
increases in concentration, the transcription of glucokinase increases. Here insulin is the
inducer.
Repression, in metabolism, is a control mechanism in which a protein molecule, called a
repressor, prevents the synthesis of an enzyme by binding toand thereby impeding the
action ofthe deoxyribonucleic acid that controls the process by which the enzyme is
synthesized. Although the process has been most-studied in microorganisms, it is
believed to occur in a similar way in higher organisms. Repression occurs mostly at the
level of transcription and less at the level of translation. For example during fasting, the
concentration of glucagon increases and glucokinase is repressed. Here glucagon is the
repressor.