Presented by: Jasmin Kototan

▪ Are catalyst that increase the rate of reaction that requires low activation energy.
There are 2 Classification of enzymes: Trivial (Working) classification and the Systematic classification.
▪ Trivial (working) classification:
- The trivial name for an enzyme with an ending –ase added to the name of the substrate subject to the
action of the enzyme in question: e.g.,
1. Sucrose- sucrase
2. lactose- lactase
3. maltose-maltase
▪ The Systematic classification:
- Constructed in a more complicated manner. (1) It is made up of the names of substrates of the chemical
reaction catalyzed by the enzyme, (2) the name of the type of the catalyzed chemical reactions, and the
ending –ase.
- For example, the systematic name for the enzyme lactate dehydrogenase(LDH) is written as:
▪ Enzymes are divided into 6 Classes each with 4-13 subclasses and named accordingly by a four-digit
number.
International Union of Biochemistry (IUB) divided these enzymes based on their action into 6 major
classes.
1. Oxidoreductase/s 2. Transferase/s
3. Hydrolase/s 4. Lyase/s
5. Isomerase/s 6. ligase/s (or synthetases).

Each enzyme is assigned a 4-digit code number. (EC A.B.C.D)

The first digit defines the general type of reaction catalysed by the enzyme and ranges from one to six.
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.
- Enzymes which catalyze oxido-reduction between two substrates.
- They catalyze the transfer of hydrogen atom or oxygen atom or electrons from one substrate to
another, Oxidorecuctases can be oxidases or dehydrogenases.
AH2 + B → A + BH2
- Oxidases are enzymes involved when molecular oxygen acts as an acceptor of hydrogen or
electrons. Dehydrogenases are enzymes that oxidize a substrate by transferring hydrogen to an
acceptor that is either NAD+/NADP+ or a flavin enzyme.
- Other oxidoreductases include peroxidases, hydroxylases, oxygenases, and reductases.
- Peroxidases are localized in peroxisomes, and catalyze the reduction of hydrogen peroxide.
- Hydroxylases add hydroxyl groups to its substrates.
- Oxygenases incorporate oxygen from molecular oxygen into organic substrates.
- Reductases catalyze reductions, in most cases reductases can act like an oxidase
▪ Important role in both aerobic and anaerobic metabolisms.
Enzymes catalyzing the transfer of a group, other than hydrogen between a pair of substrate.
AX + B → BX + A The donor is a
cofactor (coenzyme)
Classification of transferases into subclasses
charged with the
group to be
transferred.
- An enzyme that catalyze hydrolytic reaction of C-O, C-N, C-C and some other bonds. The use of water
to cleave chemical bonds.
A-B + H2O → AH + BOH
Classification of Hydrolases into subclasses
EC 3.1: ester bonds (esterases: nucleases, phosphodiesterases, lipase, phosphatase)
EC 3.2: sugars (DNA glycosylases, glycoside hydrolase)
EC 3.3: ether bonds
EC 3.4: peptide bonds (Proteases/peptidases)
EC 3.5: carbon-nitrogen bonds, other than peptide bonds
EC 3.6: acid anhydrides (acid anhydride hydrolases, including helicases and GTPase)
EC 3.7: carbon-carbon bonds
EC 3.8: halide bonds
EC 3.9: phosphorus-nitrogen bonds
EC 3.10: sulphur-nitrogen bonds
EC 3.11: carbon-phosphorus bonds
EC 3.12: sulfur-sulfur bonds
EC 3.13: carbon-sulfur bonds
- Hydrolases carry out important degradative reactions in the body. During digestion, lipases hydrolyze
lipids and proteases convert protein to amino acids.
Enzymes cleaving C-C, C-O, C-N, and other bonds by elimination, leaving double bonds or rings, or
conversely adding groups to double bonds. The systematic name is formed according to the pattern
substrate group-lyase.

Classification of Lyases into subclasses

EC 4.1 includes lyases that cleave carbon–carbon bonds, such as decarboxylases (EC 4.1.1), aldehyde
lyases (EC 4.1.2), oxo acid lyases (EC 4.1.3), and others (EC 4.1.99)
EC 4.2 includes lyases that cleave carbon–oxygen bonds, such as dehydratases
EC 4.3 includes lyases that cleave carbon–nitrogen bonds
EC 4.4 includes lyases that cleave carbon–sulfur bonds
EC 4.5 includes lyases that cleave carbon–halide bonds
EC 4.6 includes lyases that cleave phosphorus–oxygen bonds, such as adenylyl cyclase and guanylyl
cyclase
EC 4.99 includes other lyases, such as ferrochelatase
▪ An enzyme that catalyse geometric or structural changes within one molecule. According to the type of
isomerism, they may be called racemases, epimerases, cis-trans-isomerases, isomerases,
tautomerases, mutases or cycloisomerases. Mirror image of the structure
A-B → B-A
▪ are a general class of enzymes that convert a molecule from one isomer to another.
▪ Catalyze reactions across many biological processes, such as in glycolysis and carbohydrate
metabolism.
E.g., Glucose isomerase (also known as xylose isomerase) catalyzes the conversion of D-xylose and D-
glucose to D-xylulose and D-fructose.
▪ Enzymes catalysing the joining together of two molecules coupled with the hydrolysis of a diphosphate
bond in ATP or a similar triphosphate.
Classification of Ligases into subclasses
EC 6.1: includes ligases used to form carbon-oxygen bonds
EC 6.2: includes ligases used to form carbon-sulfur bonds
EC 6.3: includes ligases used to form carbon-nitrogen bonds (including argininosuccinate synthetase)
EC 6.4: includes ligases used to form carbon-carbon bonds
EC 6.5: includes ligases used to form phosphoric ester bonds
EC 6.6: includes ligases used to form nitrogen-metal bonds,
as in the chelatases
▪ Biochemistry: Guided lecture for preliminary topic (found in GCR) by
Eduardo D. Danda

▪ https://www.slideshare.net/HarinathaReddyA/classification-and-
nomenclature-of-enzymes-250264299

▪ https://www.slideshare.net/usmanqamar127/classification-and-
nomenclature-of-enzymes-40985723

▪ https://www.slideshare.net/namarta28/enzyme-classification-
233990445