Classification of enzymes:

1. Oxidoreductases- oxidation reduction/reactions.

This type of enzymes catalyze a verity of oxidation-reduction reactions
(transfer of electrons).

 Subclasses:
- Dehydrogenases: catalyze transfer of 2 hydrogen atoms H2
(alchohol:NAD+)
- Oxygenases: catalyze the incorporation of 1 or 2 oxygen atoms,
into the substrate (monooxygenases, dioxygenases) (EC 1.1.1.1.)
- Oxidases: catalyze the transfer of electrons between substrate
(like cytochrome- C oxidases, ferroxidase)
- Peroxidases: catalyze the breakdown of peroxides

2. Transferases – transfer of functional groups.

"Catalyzing transfer of groups between donors and acceptors"

 Subclasses:
- Aminotransferases
- Methyltransferases
- Glucosyltransferases
- Phosphatases- catalyze the transfer of phosphate group with a
molecule.
- Kinases: catalyze the transfer of a phosphoryl group (PO3) from
ATP to substrate (e.g. hexokinase, proteinkinases)
3. Hydrolases – hydrolysis reaction (cleavage and introduction of water).
"Hydrolytically cleaves C-O, C-N, C-C bonds, formed by condensation and
some other bonds (e.g. peptide, glycoside. Ester)"

- Esterases: e.g. lipases, phospholipases, ribonucleases and

phosphatases.
- Glycosidases: e.g. sucrase, maltase, lactase and amylase.
- Proteinases and peptidases: e.g. pepsin, trypsin, dipeptidases,
carboxypeptidases and aminopeptidases.
- Amidases: e.g. glutamines and asparginase
- ATPase: split anhydride bonds of ATP

4. Lyases – (synthases) group elimination to form double bond.

" catalyzing lysis of substrate (C-C, C-O, C-N), and generating a double bond
or rings (nonhydrolytic, and non-oxidative reactions)

 Subclasses:
- Amonialyses
- Decarboxylases: amino acids amine + co2 (elimination CO2)
- Aldolases: catalyze aldocleavage and formation
- Dehydrotases: elimination H2O (co2 + H2O H2CO3)

5. Isomerases – isomerization (intramolecular rearrangements.

" They catalyze intra-molecular transfers of atoms and their groups."

 Subclasses
- Epimerase
- Isomerase
- Mulases
 6. Ligases – (synthetases) bond formation coupled with ATP hydrolysis.
"Catalyzing racemization of optical or geometric isomers".

 Subclasses
- Glutamine synthetase
- Acetyl CoA carboxylase
- Succinate thiokinase

** synthase (lyase)- is an enzyme that catalyze a reaction in which a molecule

is synthesized, noy necessarily by forming a bond between two molecules
(unlike synthetase)

7. Translocases – is a general term for a protein that assist in moving another

molecule, usually across a cell membrane.

Molecule structure
Coenzyme Q

How Ubiquinone change to hydroquinone?

 For ubiquinone transfer to hydroquinone he first of all need to
transfer into ubisemiquinon.
The ubiquinon does that by removing..
-ubiquinon is the fully oxidized state of Coenzyme Q
- Hydroquinone is the fully reduced state of Coenzyme Q
- ubsemiquinon is the intermediate radical of Coenzyme Q.

1. Coenzyme Q- is a unique carrier for two-electron transfer within the

lipid phase of the mitochondrial membrane.(the bigger function is that
he helps to convert food into energy)  
2. The source of Coenzyme Q is in meat, fish and nuts.