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OF ENZYMES
ENZYMES
• Biological catalysts which speed up the rate of reaction
without becoming part of the reaction but themselves cannot
initiate any chemical reaction.
• Enzymes :
• First name is of substrate
• second, ending in “ASE” indicating type of reaction catalyzed.
• Clarify the reaction , e.g. Malic Enzyme
• L- Malate + NAD Pyruvate + NADH-H + CO2
• Malate NAD oxidoreductase (Decarboxylating)
Trival name
• Gives no idea of source, function or reaction
catalyzed by the enzyme.
• Example: trypsin, thrombin, pepsin.
Systematic Name
• According to the International union Of
Biochemistry an enzyme name has two parts:
-First part is the name of the substrates for
the enzyme.
-Second part is the type of reaction catalyzed
by the enzyme.This part ends with the suffix
“ase”.
Example: Lactate dehydrogenase
EC number
• Enzymes are classified into six different groups
according to the reaction being catalyzed.
• The nomenclature was determined by the Enzyme
Commission in 1961 (with the latest update having
occurred in 1992), hence all enzymes are assigned an
“EC” number.
• The classification does not take into account amino
acid sequence (ie, homology), protein structure, or
chemical mechanism.
EC numbers
• EC numbers are four digits, for example a.b.c.d, where
“a” is the class, “b” is the subclass, “c” is the sub-
subclass, and “d” is the sub-sub-subclass. The “b” and
“c” digits describe the reaction, while the “d” digit is
used to distinguish between different enzymes of the
same function based on the actual substrate in the
reaction.
• Example: for Alcohol:NAD+oxidoreductase EC
number is 1.1.1.1
CLASSIFICATION OF ENZYMES
Formulated by the enzyme commission of I.U.B six major
classes based on the type of reactions catalyzed( 7 class
1. Oxidoreductases
• Catalyzing oxidation reduction reactions
2. Transferases
• Catalyzing group transfer
3. Hydrolases
• Catalyzing hydrolytic breakdown
Classification of Enzymes
4. Lyases
• Catalysing removal of groups by mechanism other than
hydrolysis and leaving behind double bonds
5. Isomerases
• Catalysing interconversion of isomers
6. Ligases
• Catalysing formation of bonds and new compounds
1. Oxidoreductases
– Catalysing oxidation reduction reaction where one
substrate is oxidized and other is reduced
CLASSIFICATION OF ENZYMES
Ascorbic acid
Oxidase
Ascorbic acid + O2 Dehydro ascorbic
acid
CLASSIFICATION OF ENZYMES
Aerobic Dehydrogenases.
Catalyzing oxidation of the substrate and molecular
oxygen acts as recipients of hydrogen e.g. Glucose
oxidase, L amino acid dehydrogenase, Xanthene
dehydrogenase
glucose oxidase
Glucose Gluconolactone
CLASSIFICATION OF ENZYMES
Anaerobic Dehydrogenases. Catalyzing oxidation of
the substrate and coenzymes act as recipients of hydrogen
e.g. Lactate Dehydrogenase with NAD and Glucose 6
phosphate dehydrogenase with NADP
Lactate
dehydrogenase
Lactic acid Pyruvic acid
+ NAD + NADH – H+
CLASSIFICATION OF ENZYMES
Oxygenases:
Is an enzyme that oxidizes a substrate by transferring
the oxygen from molecular oxygen O2 (as in air) to it.
Types :
a. Monooxygenases:
Transfer one oxygen atom to the substrate, and reduce the
other oxygen atom to water.
b. Dioxygenases:
Incorporate both atoms of molecular oxygen (O2) into the
product(s) of the reaction.
Among the most important monooxygenases are
the cytochrome P450 oxidases, responsible for breaking
down numerous chemicals in the body.
2.TRANSFERASES
Transaminases. Catalyzing transfer of amino group between
an amino acid and a ketoacid e.g. Aspartate transaminase (AST),
Alanine transaminase (ALT)
Aspartate
transaminase (AST)
Glutamic acid + ketoglutaric
acid +
Oxalo acetic acid Aspartic acid
Alanine
transaminase (ALT)
Glutamic acid + ketoglutaric
acid +
Pyruvic acid Alanine
2.TRANSFERASES
Transmethylases. Catalyzing transfer of methyl group between
to substrates e.g. COMT
Catechol-O-
methyltransferase (COMT)
Noradrenalin Adrenaline
+ CH3
Transpeptidases. Catalyzing transfer of amino acids to
substrates e.g. Benzyl-SCoA transpeptidase
Benzyl-SCoA
transpeptidase
Benzyl - SCoA Hippuric acid
+ Glycine
2. TRANSFERASES
Phosphotransferases. Catalyzing transfer of phosphate
group to substrates e.g. Hexokinase, glucokinase
2. Oligosaccharidases
Dextrins Dextrinase glucose
3. Disacharidases
Maltose, Lactose, Sucrose Disacharidases Maltase, Lactase, Sucrase
monosaccharides
Enzymes Hydrolyzing Lipids
Triacyl glycerol lipase monoacyl glycerol + 2 F.F.A
Lecithin Lysolecithin
Enzymes Acting on Peptide Bonds:
2. Phosphodiesterases:
Removal of phosphate Group of diesters breakdown of 3’-5’ p
linkages in cyclic AMP
4. LYASES
• Catalysing reactions in which groups are removed without
hydrolysis leaving a double bond or add groups to already existing
double bonds.
Fatty acid + CoA + ATP Acyl CoA Acyl CoA (Activated fatty acid) + AMP + PiPi
Synthetase
ATP + -L-glutamyl-L-cysteine + glycine ADP + phosphate + glutathione
EC 7.Translocases
• Catalyze the movement of ions or molecules across
membranes or their separation within membranes
• E.g, Although the hydrolytic reaction is not the
primary function, several of these enzymes are
involved the hydrolysis of ATP had been previously
classified as ATPases (EC 3.6.3.-). Nowadays, these
enzymes have been classified under a new EC class
of translocases (EC 7).