HYDROLYSIS- hydrolysis of a substrate can be defined as its reaction with
water. It is a chemical process in which a molecule is cleaved into two fragments
by the addition of a molecule of water. One fragment of the parent molecule gains
a hydrogen ion (H+), while the other group collects the remaining hydroxyl group
(OH−)
Hydrolysis reactions can be the reverse of a condensation reaction in which two
molecules join into a larger one and eject a water molecule
HYDROLASES- Hydrolases are hydrolytic enzymes that use water to catalyze the
cleavage of chemical bonds, usually breaking a large molecule into two smaller
molecules.
SOME POINTS ABOUT HYDROLASE ENZYMES
Hydrolases are involved in a variety of biological processes, including
digestion, metabolism, signal transduction and regulation of cellular
activities. The natural function of most hydrolases is digestive to break down
nutrients into smaller units for digestion. For example, proteases hydrolyze
proteins to smaller peptides and then to amino acids, and lipases hydrolyze
lipids (triglycerides) to glycerol and fatty acids.
Hydrolases are classified as EC 3 in the EC number classification of
enzymes. Hydrolases can be further classified into 13 subclasses, based upon
the bonds they act upon
There are certain characteristics make hydrolases useful to the organic
chemist like broad substrate specificity, high stereoselectivity, do not
require cofactors and they tolerate the addition of water-miscible solvent,
extracellular enzymes so that they can be easily purified etc.
Systematic names of hydrolases are formed as "substrate hydrolase."
However, common names are typically in the form "substrate base". For
example, a nuclease is a hydrolase that cleaves nucleic acids.
the chemical reactions of hydrolases can be generalized as below:
A−B+H2O→A−OH+B−H
where A-B is a chemical bond in a molecule.
Some examples of hydrolase enzymes
triacylglycerol lipase- The enzyme is found in diverse organisms including
animals, plants, fungi, and bacteria. It hydrolyses triglycerides into
diglycerides and subsequently into monoglycerides and free fatty acids. EC
3.1.1.3
triacylglycerol + H2O ⇌ diacylglycerol + a carboxylate
Mechanism of working-The enzyme is highly soluble in water and acts at
the surface of oil droplets. Access to the active site is controlled by the
opening of a lid, which, when closed, hides the hydrophobic surface that
surrounds the active site. The lid opens when the enzyme contacts an oil-
water interface (interfacial activation). The pancreatic enzyme requires a
protein cofactor, namely colipase, to counteract the inhibitory effects of bile
salts
Glucose-6-phosphatase(EC 3.1.3.9)-Glucose-6-phosphatase breaks down
glucose-6-phosphate to glucose and inorganic phosphate and is the only
enzyme that is capable of forming significant amounts of glucose in the
body for use by other tissues. During fasting, adequate levels of blood
glucose are assured by glucose liberated from liver glycogen stores by
glycogenolysis as well as glucose generated by gluconeogenesis in the liver
as well as - to a lesser extent - the kidneys. G6P is the product of both these
pathways[1] and must be converted to glucose before it can be exported this
function is performed by glucose 6 phosphate
A number of isoforms of glucose 6-phosphatase have been documented in
humans, including glucose 6-phosphatase-α (G6PC), glucose 6-phosphatase-
2 (G6PC2), and glucose 6-phosphatase-β (G6PC3), it is a membrane-bound
enzyme, being associated with the endoplasmic reticulumSubstrate would be
provided to this enzyme by a translocase that is specific for glucose 6-
phosphate, thereby accounting for the specificity of the phosphatase for
glucose 6-phosphate in intact microsomes. Distinct transporters would allow
inorganic phosphate and glucose to leave the vesicles.
Applications of Hydrolases in Research and Industry
Pharmaceutical Industry- Hydrolases play a critical role in drug development and
manufacturing eg Esterases and proteases are involved in the metabolism of prodrugs,
converting them into their active forms. This property is exploited in the design of
enzyme-activated drugs.
Environmental Biotechnology-Hydrolases have significant applications in environmental
protection and sustainability eg Hydrolases, such as lipases and esterases, are used in
the biodegradation of environmental pollutants, including oils, plastics, and pesticide
Food and Beverage Industry -Hydrolases are widely used in the production and
processing of food and beverages eg Esterases and glycosidases are used to enhance
flavor in foods by releasing aromatic compounds from precursors.
