Biochemestry 3 Assignment

BIOCHEMESTRY 3 ASSIGNMENT
DUKE RACHAMI
HSP201-0015/2023
Lecturer; Dr Gervason moriasi
1 Discuss. In details the different types of inhibition in enzymes

A Competitive inhibition
It is also known as reversible Inhibition. In this type of inhibition the enzyme-inhibitor complexes are
formed during the reaction, however it depends on
 time of reintubation of enzyme with the substrate

 affinity between enzyme and substrate
When the concentrated substrate is increased the effect of inhibitor can be reversed forcing out of from
EL complex
Example Allopurinol: a drug used for treatment of gout.
B NON-competitive inhibition-there are two different types,
 Reversible
 Irreversible
The inhibitor may combine with both free enzyme and ES complex which would probably change the 3D
structure of the enzyme inactivating it catalytically .In non-competitive inhibition Vmax is lowered but
Km is kept constant .If the inhibitor can be removed from its site of binding without affecting the activity
of the enzyme is called Reversible noncompetitive inhibition. If the inhibitor is removed and causes
enzymatic reaction it is called irreversible non –competitive inhibition
Example Fluoride: inhibits the enzyme enolase by removing magnesium ions and manganese ions which
stops glycolysis
C Allosteric Inhibition
There is a mixed kind of inhibition when the inhibitor binds to the enzyme –substrate complex forming
an inhibitor enzyme substrate complex. This type of inhibition is unique because it requires the
substrate to be bound to the enzyme before the inhibitor can bind .it results in a decrease in the
maximum velocity of the binding of the substrate to the enzyme.
D Suicide Inhibition
Is a special type of inhibition where the substrate analogue is converted to a more effective inhibitor
with the enzyme to be inhibited? The so formed substrate new inhibitor binds irreversibly with the
enzyme.
ExampleAsprin: a: a: a drug used for relieving pain.

E uncompetitive inhibition
Occurs when the inhibitors binds only to the enzyme –substrate complex forming an inhibitor enzyme
substrate complex. This type of inhibition is unique because it requires the substrate to be bound to the
enzyme before the inhibitor can bind. It results in a decrease in decrease in the maximum velocity of the
reaction and does not affect the binding of the substrate to the enzyme.
2 Discuss in details the mechanisms through which enzymes are

regulated (providing real life examples)
Ubiquitin –proteasome pathway is one the mechanism through which enzymes are regulated.
Thus the ubiquitin-proteasome pathway can selectively degrade proteins whose physical integrity and
fictional competency has compromised:
 By the loss of or damage to a prosthetic group.

 Oxidation of cysteine or histidine residues.
 Deamination of asparagine’s or glutamine residues.
Recognition by proteolytic enzymes also can be regulated by covalent modification such as

phosphorylation binding of substrates or allosteric effectors or association with membranes
oligonucleotides or other proteins.
Example: streptokinase and urokinase: it: it increases the conversion of plasminogen to plasmin which
later breakdown fibrin to attain thrombolysis.
3 Discuss in details the role of enzymes in pharmacology

Systemically used enzymes include:
 Streptokinase
 It is used to increase the circulating level of plasminogen
 An indicator is acute myocardial infarction.
 L-asparagine
 Certain tumors cells require it for growth .L-asparagine also enables hydrolases.
 Some of its indicators include acute leukemia and malignant lymphomas.
 Amylase, Lipase and protease
Replacement therapy in pancreatic insufficiency some of its indicators include
 Cystic fibrosis
 Chronic pancreatitis
 Serratopeptidase
 Exhbits its fibrinolytic activity high bradykinin decomposing activity and potent casein lytic
activity.
 An indicator is subconjuctal bleeding.
Enzymes used in the laboratory as reagent

 Glucose oxidase- used for estimation of true glucose in blood and body fluids.
 Enzyme Uri case- used in estimation of serum uric acid
 Enzyme urease- used for estimation of urea in blood and body fluids
Enzymes used locally
 Hyaluroniclase- it brings about depolymerisation of ground substance and helps in absorption of

fluids.
 An indicator is that it promotes diffusion of fluids.

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BIOCHEMESTRY 3 ASSIGNMENT

Lecturer; Dr Gervason moriasi

1 Discuss. In details the different types of inhibition in enzymes

 time of reintubation of enzyme with the substrate

Example Allopurinol: a drug used for treatment of gout.

B NON-competitive inhibition-there are two different types,

ExampleAsprin: a: a: a drug used for relieving pain.

2 Discuss in details the mechanisms through which enzymes are

 By the loss of or damage to a prosthetic group.

Recognition by proteolytic enzymes also can be regulated by covalent modification such as

3 Discuss in details the role of enzymes in pharmacology

Replacement therapy in pancreatic insufficiency some of its indicators include

Enzymes used in the laboratory as reagent

Enzymes used locally

 Hyaluroniclase- it brings about depolymerisation of ground substance and helps in absorption of

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