FACTORS EFFECTING ENZYME ACTION
pH:
Enzymes are affected by changes in pH. The most favorable pH value - the point where
the enzyme is most active - is known as the optimum pH.
Extremely high or low pH values generally result in complete loss of activity for most
enzymes.
Most of the enzymes of higher organisms work near neutral pH (6-8) but there specific
enzyme which work at optimum PH (Saliva amylase 6.8 PH). There are, however, many
exceptions like pepsin (1-2), acid phosphatase (4-5) and alkaline phosphatase (10-11) for
optimum pH.
Different enzyme has different optimum pH. Beyond the optimum ph the change in the
ion leads to denaturation of the enzyme.
Remark:Different enzyme has different optima PH.
All enzym has same temperature optima
Concentration of Substrate: Increase in the substrate concentration gradually
increases the velocity of enzyme reaction within the limited range of substrate levels.
Increasing Substrate Concentration increases the rate of reaction. This is because more
substrate molecules will be colliding with enzyme molecules, so more product will be
formed.
However, after a certain concentration, any increase will have no effect on the rate of
reaction
Enzyme kinetics and Km value:
The enzyme (E) and substrate (S) combine with each other to form an unstable enzyme-
substrate complex (ES) for the formation of product (P).
Here k1, k2 and k3 represent the velocity constants for the respective reactions, as
indicated by arrows.
Km, the Michaelis-Menten constant (or Brig’s and Haldane’s constant), is given by the
formula
where v = Measured velocity,
Vmax = Maximum velocity,
S = Substrate concentration,
Km = Michaelis-Menten constant.
Km or the Michaelis-Menten constant is the molar conc. Of the substrate at which
Vmax
is attained.
2
Km value is a constant and a characteristic feature of a given enzyme. It is a
representative for measuring the strength of ES complex. A low K m value indicates a
strong affinity between enzyme and substrate, whereas a high K m value reflects a weak
affinity between them. For majority of enzymes, the K m values are in the range of 10-5 to
10-2moles.
INHIBITION OF ENZYME ACTION
COMPETITIVE INHIBITION: Competitive inhibition is a form of enzyme inhibition where
competition takes place in between inhibitor and substrate.
E.g: 1. Succinate changes into fumarate by succinate dehydrgenase .if
malonate is added, then 50% of enzyme site is occupied by malonate and
remains by succinate. In first time fumarate go down by 50% approximately.
And finally very less fumarate would be synthesized
E.g: 2. PABA is converted into folic acid which is required for normal growth
and reproduction of bacteria by the enzyme foilc acid synthetase. If sulpher
drugs is added then very low amount of folic acid is produced
If the substrate conc. Is very high in compare to inhibitor then inhibitor
dislodge from active site and reaction will be reversed (Reversible type)
NONCOMPETITIVE INHIBITION: The inhibitor does not compete with substrate ..it is a
irreversible process.
Substrate structure are complementary to active site but inhibitor does not has.
Inhibitor bind to anywhere of enzyme
binding of inhibitor to enzyme leads to confirmational changes of active site
Enzyme substrate complex will never form
No product will formed
E.g- cyanide: binds to cytochrome oxidase( important for cellular respiration).if cellular
respiration stops then the cells activity will also stop and leads to instant death.
Penicillin: it is non competitive inhibitor of enzyme required for cell wall formation in bacteria.
ALLOSTERIC INHIBITION: It is also called feedback mechanism. The product
regulates its own formation or conc. by stimulating or affecting the enzyme. If product
increase or decrease the enzymatic activity then it is called positive or negative feedback
mechanism.
NOMENCLATURE OF ENZYME
Putting the suffix ‘ase’ to the root word. Maltose maltase. Sucrose sucrase .
Naming the enzyme on the basis of source. Bromalin is found in pine apple ,bromeleasea .
papain- obtain from papaya
Two word. First one to the substrate and second one is to the reaction .e.g –pyruvate
decarboxylase - removing carbon from pyruvate
E.C no- enzyme commissions no six groups. Given by international union of biochemistry. .
EC 1 – oxydoreductase
EC 2-transferase
EC 3-hydrolases
EC 4-lyases
EC 5-isomerases
EC 6 –ligases
Oxidoreductases: cytochrome oxidase- helps in electron transport chain
phosphoglycelordehydehydrogenase- helps in glycolysis
Transferase : naming after which functional group transfer .
Alani
Glu Pyr ne +
ta Alpha
uv ketog
ma
te ate lutam
ate
glutamate pyruvate transferase help in this reaction
Hydrolases : Break the bond with addition of water.
Digestive enzyme .starch is broken down into maltose, iso-maltose and lipid dextrin by
the enzyme amylase.
Lyases: make bond without addition of water. E.g-aldolase
Isomerases: glucose 6 phosphate is transfer to fructose 6 phosphate by glucose fructose
isomerase
Ligase: it is joining enzyme . helps in formation of new bond pyruvic acid and carbone di oxide
transfer to oxalo acetic acid by the enzyme pyruvate carboxylase.
IMPORTANT THINGS ABOUT
ENZYME
Inactive enzyme are known as proenzyme or zymogen
isoenzymes or isozymes-they have slightly different molecular structure but help in same
reation .e.g- lactic dehydrogenase
rennet tablets:secrete in the stomach of calf. Used for cheese making . comprises of multiple
enzyme with gastir juice
turn over no- no of substrate molecule acted upon by one enzyme molecule in man . for
carbonic anhydrase the no is- 6m
fastest enzyme - carbonic anhydrase- helps in formation and breakdown of carbonic acid
slowest enzyme- lysozyme –present in tears saliva
largest enzyme- catalase- found in peroxisome
smallest enzyme-peroxidase or oxidase