The document discusses enzyme kinetics, focusing on the Michaelis-Menten model and the significance of parameters such as Vmax and Km. It describes the Lineweaver-Burk plot as a method for accurate determination of Vmax and applications in drug metabolism. The study highlights the relevance of enzyme kinetics in understanding metabolic processes in living organisms.

1. GURU NANAK INSTITUTE OF PHARMACEUTICAL SCIENCE AND
TECHNOLOGY (An Autonomous Institute)
TOPIC :ENZYME KINETICS
NAME OF THE STUDENT: MD JAVED
ROLL NO: 186112201008
ACADEMIC SESSION: 2022-2024
PAPER NAME: Advanced Medicinal
Chemistry
PAPER CODE:MPT 1033
Affiliated to MaulanaAbul KalamAzad University of Technology

2. CONTENTS
1. Introduction
2. Michaelis-menten Model
3. Significance
4. Lineweaver-burk plot.
5. Future prospect of Enzyme kinetics
6. Summary
7. Reference

3. INTRODUCTION
 The study of rate at which an enzyme works is called enzyme kinetics.
 It was developed by Leonor Michaelis,Maud Menten in 1913.
 Two constant Vmax and Km play an important role.
 E + S ↔ ES ↔ E + P where E is enzyme, S is substrate, ES is enzyme substrate
comples and P is product.
 Different theories have been plot by have been proposed by various scientist like
Michaelis-menten plot and Line-Weaver Burk plot.(1)

4. MICHAELIS-MENTEN MODEL
• Enzyme involves invertase in reaction.
• It degrades sucrose to glucose and fructose.
• Relation between reaction velocity and substrate concentration.
• Hyperbola curve.(2)

5. Significance of Km
• Km is the substrate concentration that gives half of the maximal velocity.
• Km is the Michaelis-constant which varies from enzyme to enzyme(value).
• Km depends upon nature of substrate pH, ionic strength and on temperature.
Significance of Vmax
• the maximum rate of reaction when all enzyme active sites are satuated with
substrate.
• it reveals the turnover number of an enzyme.(2)

6. • Vo=Vmax(
𝑺𝑼𝑩𝑺𝑻𝑹𝑨𝑻𝑬
𝑺𝑼𝑩𝑺𝑻𝑹𝑨𝑻𝑬 +𝑲𝒎
) is the Michaelis-menten equation where Vo is
the intial velocity of reaction , Vmax is the maximum rate of reaction and Km is the
Michaelis-menten constant.(3)
• Taking the reciprocal of both side of the Michaelis-Menten equation to determined
the values of KM and Vmax. The double-reciprocal of Michaelis-Menten equation:-

7. LINEWEAVER-BURK PLOT
• Double reciprocal plot
• Plot between the reciprocal of V and S
• Used to find the accurate value of Vmax.
• Accurate plot to get the exact value.(4)
• Significance of plot is to determined the inhibition.(competitive and non competitive)

8. FUTURE PROSPECT OF ENZYME KINETICS
 Knowledge about enzyme kinetics can reveal useful info about role in metabolism,
how the enzyme works and how it behaves in living species.
 Studies are being done to get info about diverse range of reaction in human body.(1)

9. SUMMARY
• Kinetic study helps in understanding drug metabolism.
• Since enzyme activity is affected by concentration, pH etc. studying kinetics might
help in providing suitable for drug to be efficient.
• Lineweaver-burk plot has great advantage of allowing accurate determination of
Vmax.

10. REFERENCE
1) Nagar, S., Argikar, U. A., & Tweedie, D. J. (2014). Enzyme Kinetics in Drug Metabolism:
Fundamentals and Applications. Methods in Molecular Biology, 1–6.
https://doi.org/10.1007/978-1-62703-758-7_1.
2) Structural Biochemistry/Enzyme/Michaelis and Menten Equation - Wikibooks, open books
for an open world. (n.d.). Retrieved September 24, 2022.
3) Libretexts. (2021, August 24). 7.2: Derivation of Michaelis-Menten equation. Biology
LibreTexts. Retrieved September 24, 2022.
4) Rodriguez, J. M. G., Philips, S. J., & Towns, M. H. (2019, August 6). Michaelis–Menten
Graphs, Lineweaver–Burk Plots,: Investigating Introductory Biochemistry Students’
Conceptions of Representations in Enzyme Kinetics. Journal of Chemical Education, 96(9),
1833–1845. https://doi.org/10.1021/acs.jchemed.9b00396.