Biochemistry Report

Q3/explain brifely Hydrolases

Hydrolases are hydrolytic enzymes, biochemical catalysts that
use water to cleave chemical bonds, usually dividing a large
molecule into two smaller molecules. Examples of common
hydrolases include esterases, proteases, glycosidases,
nucleosidases, and lipases.

Hydrolases carry out important degradative reactions in the

body. During digestion, lipases hydrolyze lipids and proteases
convert protein to amino acids. Hydrolases cleave large
molecules into fragments used for synthesis , the excretion of
waste materials, or as sources of carbon for the production of
energy. In these reactions, many biopolymers are converted to
monomers. Some hydrolases release energy as they act.

One of the most important hydrolases is acetylcholine esterase

(cholinesterase). Acetylcholine is a potent neurotransmitter for
voluntary muscle. Nerve impulses travel along neurons to the
synaptic cleft , where acetylcholine stored in vesicles is
released, carrying the impulse across the synapse to the
postsynaptic neuron and propagating the nerve impulse. After
the nerve impulse moves on, the action of the neurotransmitter
molecules must be stopped by cholinesterase, which hydrolyzes
acetylcholine to choline and acetic acid. Some dangerous toxins
such as the exotoxin of Clostridium botulinum and saxitoxin
interfere with cholinesterase, and many nerve agents such as
tabun and sarin act by blocking the hydrolytic action of
cholinesterase.