Starting of enzymology useful for B.SC and M.SC students.

1. HISTOLOGICAL
DEVELOPMENT IN
ENZYMOLOGY
Presented by:
RUPAL AGRAWAL
16SOSMB21001
SCHOOL OF SCIENCE
R.K.UNIVERSITY

2. INTRODUCTION:
• Enzyme, in Greek means in living (en= in, zyme= living).
• Biocatalysts or Organic catalysts, usually high molecular
weight proteins ( exception- Ribozymes or RNA
enzymes).
• Term was coined by Kuhne in 1878.
• First enzyme to be extracted from Yeast cells by
Eduard Buchner ( 1897) was zymase.
• First purified enzyme is Urease, by James B.
Summer (1926).
Eduard Buchner

3. 700BC
• Homer’s lliad:
• As the juice of fig tree curdles milk, and thickens it in a moment
though it be liquid, even so instantly did Paeeon cure fierce Mars
1700s
• Digestion is a chemical process and not physical was
known.
• Louis Pasteur found that there is a vital force in yeast
cells that ferment sugar to alcohol.
1800s
• Hans & Eduard Buchner- filters of yeast extract could
catalyse fermentation and there is no need of living
cells.
• E.Fischer gave” lock and key” hypothesis.

4. LOCK AND KEY HYPOTHESIS: says there is
perfect fit between active site and substrate.

5. Induced Fit Model: active site can expand
or contract to fit the substrate shape.

7. 1903
• Henri-prepared first successful
mathematical model.
1913
• Michaelis and Menten- gave equation
to calculate rate of reaction.
1965
• Monod, Wyman and Changeux-
explained allosteric regulation

8. Overview of Enzymes:
• Enzymes-are organic catalyst produced by an
organism. The reactant in an enzyme-catalysed
reaction is called substrate.
• The small portion of the molecule that is
responsible for the catalytic action of the enzyme
is the active site.

10. Activators and Inhibitors:
• Activators- inorganic substances that tends to
increase the activity of enzyme.
• Inhibitors- any substance that will make the
enzyme less active or render it inactive.
Competitive Inhibitors- binds reversibly in
the active site and so block the access by the
substrate.
Incompetitive Inhibitors- bind to another
site on the enzyme to render it less active or
inactive.

11. Mode of enzyme activity:

12. Apoenzymes and Coenzymes:
Enzymes are conjugated proteins- they contain a
protein and a non- protein part. Both parts must be
present before the enzyme can function.
The protein part is called the apoenzyme
and the non- protein ( organic part) is called
coenzyme.
coenzyme + apoenzyme = enzyme

13. Significance of enzymes:
1. Enzymes of kidney:
If an individual’s blood pressure drops, as in
case of haemorrhaging or in hypokalemia, the
kidneys secrete the enzyme renin into the blood
stream.
Angiotensinogen angiotensin I angiotensin II
Angiotensin II increases the force of the
heartbeat and constricts the arterioles, thus causing
an increase in blood pressure.
renin converting
enzyme

14. Other kidney enzyme include:
• Glucose-6-phosphate : involved in the removal of
the phosphate group from glucose-6-
phosphate,enabling glucose to diffuse from the cell
into blood stream.
• Glutaminase : involved in the conversion of
glutamine into glutamic acid.
• Hydroxylase : involved in the synthesis of calcitriol.

15. 2. Enzymes used in chemotherapy:
One of the most promising new
chemotherapeutic agent in decades is taxol, a
natural product obtained from the bark of pacific
yew trees.
Taxol acts by interfering with
cellular growth and function and is very effective
in shrinking a variety of tumors, particularly in
advanced cases of ovarian and breast cancer.

16. Recent applications of enzymes in
research field.
• Applications of enzymes in synthetic carbohydrate
chemistry. J Thiem - FEMS microbiology reviews,
1995 – Elsevier.
• Potential applications of enzymes immobilized
on/in nano materials: a review
SA Ansari, Q Husain - Biotechnology advances,
2012 - Elsevier