ENZYMES ( In yeast)

Payen discovered the first enzyme Called Diastase also called α. amylase
(Ptyalin) acts on Starch and Convert it into maltose. It is also found in saliva.
1878 Wilhelm Kuhne used the word enzyme for the first time.
Characteristics of Enzymes
Enzymes are organic molecules that speed up chemical reaction without being
consumed.
Mostly enzymes are consist of Globular Proteins with 3D Tertiary/Quaternary
Structure but there are some enzymes consist of RNA only Called Ribozyme
found in Ribosome such as Peptidyl transferase that form Peptide bonds b/w
Amino acids during translation.
The molecules on which enzyme work Called Substrate.
Enzymes are greater in size than substrate.
Enzymes are either consist of protein e.g. amylase and pepsin or may
contains, along with protein, a non-protein part .e.g. Acetyl CoA.
STRUCTURE OF ENZYME
Active site Each enzyme has one or more Specific Charge bearing three
dimensional Cavities, where Substrate can bind with Еnzyme. The
Substrate molecule attached to the A. Site by non Covalent
interactions like hydrogen bonding and hydrophobic interactions.
Active Site Consist of 3-12 Amino acids ,as A. Site for Aldolase enzyme
Consist of glycine, histidine and alanine amino acids.
Components of A. site : Consist of 2 Parts. a. Binding Site : Where
Substrate attaches with enzymes
b.catalytic site : Where Catalysis of Substrate takes place
Chemical nature / component of enzymes
simple enzymes (proteozymes) : Enzymes that consist of only proteins
like amylase and pepsin
conjugated enzymes: (Holoenzymes ) Enzymes that consist of protein
and non protein parts. The protein part is called Apoenzyme. The non
protein part is called co factor.
Types of co factor
Inorganic co factor: Metallic ions Such as Fe, mg, zinc. They are loosely
(non covalently) attached with enzyme. They are also called Activator.
Organic co factor: a. co enzymes: Most vitamins are Co-enzymes
Such as ATP,NAD,FAD .They are detachable.
b. prosthetic group: Permanently attached (Covalently bonded) such
mg Containing Porphyrin ring chlorophyll.
The conjugated enzyme (holoenzyme) with out its co factor is
inactivated and is called Apoenzyme.
( Holoenzyme = co factor + apoenzymes)
Mechanism of enzymes action
 Models of enzyme action
lock and key Model Emil Fischer 1898.
Active site of enzyme (lock) is rigid and can fix only one Particular
Substrate (key) in it .This Model is less accepted.

Induce fit Model Daniel Koshland 1959.

A. Site is flexible , there fore more than one type of related substrates can
bind with A. site (More than one type of reaction Can be Carried out by
Same enzyme). Glove (enzyme ) and hands (substrate) .
 ACTIVATION ENERGY OF ENZYMES
Minimum Energy needed to Start Chemical reaction is called Activation
energy.
Enzymes help in lowering the Activation energy by Enabling the
reactant molecules to absorb enough energy to reach transition
State. (When molecules have absorb enough for the bonds to
break. In this State Substrate Can Change in to Products).
Lower the activation energy faster will be rate of reaction.

86 KJ/Mole
H2O2 →→→→→→ H2O + O
with out Enzyme

1 KJ/Mole
H2O2 →→→→→→ H2O + O
with Enzyme like catalase
Factors affecting enzymes activity
1.Temperature
Heat increases molecular motion. As the temp rises from 'Zero' molecules of
Substrate and enzyme will get more and more Kinetic energy so rate of reaction will
increases. For every 10°c rise in temp the enzymatic activity doubles. There is specific
temp : at which enzyme Catalytic activity is fastest and known as Optimum Temp. If
temp is increased above this level then decrease in rate of reaction will occur b/c
Tertiary and Quaternary Structure of enzyme will disrupted and enzyme will
denatured, this temp is called Max : Temp . If temp is reduced to near or below
freezing point enzymes are Inactivated not denatured. They will regain their Catalytic
influence when higher temp are restored. This thump where Inactive enzyme becomes
active again called Minimum Temp (The below graph shows increasing temp will also
increase rate of reaction but in un linear way)
2.PH
Each enzyme has an optimum PH at which it works fast. The optimum PH for
most of the enzymes is 6-8 .Pepsin 1.5 (1.5 to 2.5), Pancreatic Amylase 8.5 ,
salivary amylase 6.8,Trypsin 7.8 to 8.7 ,Maltase 6.1 to 6.8, Arginase 9.7,
Sucrase 4.5. Papain (green Papaya) Work in both acidic and alkaline.
Slight Change in optimum pH of an enzyme Causes ionization of amino acids
of enzyme and enzyme becomes Inactive temporarily. Where as extreme
Change in Optimum PH alters the ionic charge of the acidic and Basic groups
of enzyme and there fore disrupts the ionic bonding (denaturation) and
ultimately Tertiary and Quaternary Structure is affected.
3.Conce: of substrate
if enzyme conc: is constant increasing amount of substrate will increase rate of reaction but up to specific level
called saturation. after that level increase in substrate will not increase rate of reaction. very high substrate conc:
will have retarding (negative) effect on enzymes
4.conce: of enzymes
if we increase the conc: of enzymes rate of reaction will also increase but up to certain level (where amount of
enzymes and substrate become equal) after that increasing enzyme conc: will not increase rate of reaction rather
than it remains constant.
5.Enzyme Inhibitors :
The molecules that react with enzymes but are not Converted into Products are called inhibitors
such as Parathione, DDT (Dichlorodiphenyltrichloroethane) are used as insecticides but are key
inhibitors of Human Nervous System enzymes. Other inhibitors are Penicillin, cyanides,
Sulpha drugs, Phenylalanine
1.Competitive inhibitors :
They attached with active site of enzyme instead of substrate .
a.Reversible competitive inhibitors: are attached with active site of enzymes temporarily ( can leave
the active site if conc: of substrate increases) such as malonate is R.C.I for enzyme that act on
succinate.
b .Irreversible Competitive inhibitors : Inhibitors attached permanently with enzymes active site such
as DDT, parathion,sulpha drugs,antibiotics
2.Non competitive inhibitors :attached with allosteric site (other than active site)
a.Reversible non competitive inhibitors: attached temporarily. They allow enzyme substrate complex
to be formed but do not allow substrate to be converted into products. Example feed back
inhibition
b.irreversible non Competitive inhibitors : attached permanently and do not allow Enzyme substrate
complex to be formed . example cyanide, silver ,copper ,mercury.
3.Uncompetitive / anticompetitive inhibitors: is a special form of reversible noncompetitive
inhibition.it occurs when there is more than one substrate involved in reaction and the inhibitor binds
to the enzyme-substrate complex only.
Enzymes Nomenclature
Classification on the basis of reaction types
1.Oxido reductase : Catalyze oxidation/reduction of their Substrates.
2. Transferases : Catalyze transfer of specific functional group other than H from one substrate
to another. Such as Amino group, Methyl 3. Hydrolases
: Catalyze the breakdown of molecule with using H20.
4.Lyases: Catalyze the breakdown of molecule with out using H20
5.Isomerases : Catalyze the isomerism reaction.
6.Ligases (sythetase) : catalyze condensation reaction of RNA and DNA.
Classification based on Name of Substrate 1. Proteases : Breaks Protein into Amino acids. 2.
Lipases : work on lipids 3. Amylase : Break down Amylose into maltose 4. Maltase :
Convert Maltose into two alpha Glucose.
5.Glucosidase : Convert Cellubiose into two beta Glucose molecules. 6. Lactase :
Convent lactose into glucose and galactose. 7. Nucleases : Acts
on Nucleic Acid.