BIOCHEMISTRY LECTURE
DOC GOUREV K. CHAWLA
Lesson: Enzymes
Enzymes
● Biological Catalysts, speed up biochemical reactions
● High specificity, used for regulation
● not consumed in a chemical reaction
● Note: almost all enzymes are globular proteins
○ special types:
◆ abzymes - immunoglobulin (or antibodies) that act as catalysts
○ exception
◆ ribozymes - RNAs that act as catalysts
GENERAL CHARACTERISTICS OF ENZYMES
An enzyme is an organic compound that acts as a catalyst for a biochemical reaction. Each cell in the human
body contains thousands of different enzymes because almost every reaction in a cell requires its own specific
enzyme.
Enzyme structure
Enzyme Nomenclature
IMPORTANT ASPECTS IN ENZYME NOMENCLATURE
1. Suffix: "-ase".
○ Some use the suffix "-in" (e.g. trypsin, chymotrypsin, pepsin)
2. Prefix: denotes the type of reaction catalyzed (e.g. oxidase, hydrolase, ligase)
3. Identity of Substrate
Classification of enzymes
Subclasses of enzymes
Classification of enzymes
● identify the classes of enzymes involved
Enzymes catalysts
● substrate - reactant; catalyzed by enzymes
● active site - region in enzyme where the substrate attaches
● enzyme-substrate complex - the compound form by attaching the substrate into the enzyme
● Increase the reaction rate by lowering the activation energy
FACTOR AFFECTING ENZYME ACTIVITY
1. pH
○ optimum pH - pH level in which enzyme can do its maximal effect
2. Temperature
○ optimum temperature - T in which an enzyme can function at maximal activity ( in humans ~ 37C
at higher T desaturation occurs)
3. Enzyme and substrate concentration
Enzymatic browning
Enzyme catalysis
MODELS OF ENZYME ACTION
I. Lock-and- key model
◆ only a substrate whose shape and chemical nature are
complementary to those of the active site can interact
with the enzyme
2. Induced-fit model
◆ the enzyme active site is flexible enough that
it can adapt to the shape of the substrate
Enzyme inhibition
Enzyme inhibitors - molecular agents that interfere with catalysis, slowing or stopping enzymatic reactions
1. Irreversible inhibition
◆ inhibitors bind covalently with an enzyme's active site ( e.g. Nerve gases, organophosphates)
2. Reversible inhibition
◆ temporary loss of enzyme activity; noncovalent
bonding of enzyme with hibitor
Reversible enzyme inhibition
Enzyme regulation
Allosteric enzymes have 2 kinds of binding sites:
1. Active site
◆ where substrate binds
2. Allosteric or regulatory site
◆ where regions
Regulator is a substance that binds
to an allosteric site
1. Activator
2. Inhibitor
Enzyme regulation
1. Feedback control - product controls the reaction sequence by activating or inhibiting an earlier reaction
in a pathway
&
2. Zymogens (proenzyme) - inactive precursor of enzymes
○ small part of peptide chain must be cleaved to become active
3. Covalent modification - adding or removing a functional group to an enzyme to render it either active or
inactive
○ usually through enzyme phosphorylation / dephosphonylation
4. Isoymes - multiple forms of the game enzyme
○ exist in different proportions in different tissues
○ ex. Lactate dehydrogenase enzyme in heart vs skeletal muscles
Medical application
● review some medical applications of enzyme action and inhibition:
○ therapeutic
○ diagnostic
