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Subject Code –
Course-
Submited to –
Submited by -
Hygia Institute Of Pharmacy Approved By AICTE, PCI &
Affiliated To AKTU Prabandh Nagar, IIM Road, Lucknow-
226013
Topic-Regulation of
Enzyme
01
CONTENTS
02
Introduction
Regulation of enzyme activity is important to
coordinate different metabolic processes.
03
Enzyms are regulated by
 Controlling their concentration
1. Control of synthesis (activation or repression)
2.Degradation
 Controlling the availability of substrate
1. Production, degradation, compartmentation of
substrate
2. Reversible binding of competitive inhibitors
 Controlling the activity of the enzyme
1. Reversible binding of modulators/effectors
2. Reversible or irreversible covalent modification
04
Regulatory enzymes
 These are the enzymes (2 large groups) whose activity
can be changed in response to cell needs.
 Allosteric enzymes
 Enzymes regulated by reversible covalent modification
(reversible phosphorylation, reversible acetylation
and so on)
 There are enzymes which have properties of both groups
05
 Allosteric enzymes contain two different sites:
the active site for catalysis
allosteric site for regulation
 The sites are located in distinct places of enzyme
molecule.
 Molecules that affect activity of an allosteric enzyme
bind to the allosteric site. These molecules are called
allosteric
effectors
Allosteric enzymes
06
07
Kinetics of allosteric enzymes Effects of
allosteric effectors
 Cooperative effect in multimeric enzymes.
 In a case of allosteric enzyme, the dependence of the
reaction velocity against substrate concentration is S-
shaped curve.
 Homotropic allosteric effectors (activators) are substrate
molecules.
 Heterotropic allosteric effectors are molecules different
than substrates.
08
Allosteric effectors
 Allosteric activators/ positive effectors: result in
increasing the reaction velocity and in increasing the
affinity of an allosteric enzyme to its substrate.
 Allosteric inhibitors / negative effectors: result in
decreasing the reaction velocity and in decreasing the
affinity of an allosteric enzyme to its substrate.
09
Feed-back inhibition
 A sequence of enzymatic reaction with a
particular goat is considered as a
system/pathway of enzymes.
• Feed-back inhibition is a way ofregulation
of enzymatic system activity exerted via initial enzymes of
the system. Initial
enzymes usually are allosteric 10
.
11
ANY QUERIES
12

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Shazad Regulation Of Enzyme updated 2.pptx

  • 1. Subject Code – Course- Submited to – Submited by - Hygia Institute Of Pharmacy Approved By AICTE, PCI & Affiliated To AKTU Prabandh Nagar, IIM Road, Lucknow- 226013 Topic-Regulation of Enzyme 01
  • 3. Introduction Regulation of enzyme activity is important to coordinate different metabolic processes. 03
  • 4. Enzyms are regulated by  Controlling their concentration 1. Control of synthesis (activation or repression) 2.Degradation  Controlling the availability of substrate 1. Production, degradation, compartmentation of substrate 2. Reversible binding of competitive inhibitors  Controlling the activity of the enzyme 1. Reversible binding of modulators/effectors 2. Reversible or irreversible covalent modification 04
  • 5. Regulatory enzymes  These are the enzymes (2 large groups) whose activity can be changed in response to cell needs.  Allosteric enzymes  Enzymes regulated by reversible covalent modification (reversible phosphorylation, reversible acetylation and so on)  There are enzymes which have properties of both groups 05
  • 6.  Allosteric enzymes contain two different sites: the active site for catalysis allosteric site for regulation  The sites are located in distinct places of enzyme molecule.  Molecules that affect activity of an allosteric enzyme bind to the allosteric site. These molecules are called allosteric effectors Allosteric enzymes 06
  • 7. 07
  • 8. Kinetics of allosteric enzymes Effects of allosteric effectors  Cooperative effect in multimeric enzymes.  In a case of allosteric enzyme, the dependence of the reaction velocity against substrate concentration is S- shaped curve.  Homotropic allosteric effectors (activators) are substrate molecules.  Heterotropic allosteric effectors are molecules different than substrates. 08
  • 9. Allosteric effectors  Allosteric activators/ positive effectors: result in increasing the reaction velocity and in increasing the affinity of an allosteric enzyme to its substrate.  Allosteric inhibitors / negative effectors: result in decreasing the reaction velocity and in decreasing the affinity of an allosteric enzyme to its substrate. 09
  • 10. Feed-back inhibition  A sequence of enzymatic reaction with a particular goat is considered as a system/pathway of enzymes. • Feed-back inhibition is a way ofregulation of enzymatic system activity exerted via initial enzymes of the system. Initial enzymes usually are allosteric 10
  • 11. . 11