Enzymes and living systems

Ass. prof. Nikolina Elez-Burnjaković

• All chemical reactions involved in maintaining the living state of the cells
and the organism
• A set of biochemical reactions that take place in a living system and enable
life
• Catabolism - the breakdown of molecules to obtain energy
• Anabolism - the synthesis of
all compounds needed by
the cells

METABOLISM
 Enzyme’s role in metabolism
• Catalysts – increase the rate of all chemical reactions within cells
• Proteins, ribonucelic acid

S P
PROPERTIES
E
S P

S+ E ES E+ P Increase rate of chemical

reactions without
Increase rate of chemical
reactions without altering
themselves being
chemical equilibrium
comsumed or
between reactants and
permanently altered by
products
the reaction
 Mechanisms of Enzymatic Catalysis
“Lock-and-key” model -  Emil Fischer  1890
“Induced fit” model - Daniel Koshland  1958
 Factors affecting enzyme activity
 
1. Temperature: Raising temperature generally speeds up a reaction, and
lowering temperature slows down a reaction. However, extreme high
temperatures can cause an enzyme to lose its shape (denature) and stop
working.
2. pH: Each enzyme has an optimum pH range. Changing the pH outside of this
range will slow enzyme activity. Extreme pH values can cause enzymes to
denature.
3. Enzyme concentration: Increasing enzyme concentration will speed up the
reaction, as long as there is substrate available to bind to. Once all of the
substrate is bound, the reaction will no longer speed up, since there will be
nothing for additional enzymes to bind to.
4. Substrate concentration: Increasing substrate concentration also increases the
rate of reaction to a certain point. Once all of the enzymes have bound, any
substrate increase will have no effect on the rate of reaction, as the available
enzymes will be saturated and working at their maximum rate.
 Enzyme classification
 Division according to complexity
• simple enzymes (just protein)
• complex enzymes - holoenzymes (apoenzyme – protein part bound to
its necessary cofactors or prosthetic groups)

 Division by place of action

• Endoenzyme, or intracellular enzyme (that functions within the cell in
which it was produced)
• Exoenzyme (that functions out of the cell in which it was produced)
• Zymogen also called a proenzyme, is an inactive precursor of
an enzyme.
 Coenzymes
 Prosthetic groups are small molecules bound to proteins in which they
play critical functional roles (oxygen, zinc, iron, Mg, K, Ca, Fe, Cu, Co, Mo)
 coenzymes - organic molecules participate in specific types of enzymatic
reactions
 work together with enzymes to enhance reaction rates

Coenzyme Related vitamin Chemical reaction

NAD+, NADP+ Niacin Oxidation-reduction
FAD Riboflavin (B2) Oxidation-reduction
Thiamine pyrophosphate Thiamine (B1) Aldehyde group transfer
Coenzyme A Pantothenate Acyl group transfer
Tetrahydrofolate Folate Transfer of one-carbon groups
Biotin Biotin Carboxylation
Pyridoxal phosphate Pyridoxal (B6) Transamination
 Regulation of Enzyme Activity
Optimal conditions
1. Temperature
2. pH
3. Enzyme concentration
4. Supstrate concentration
Mechanism of activation/inhibiton:
1. Allosteric regulation
2. Negativne feedback inhibition
3. Competitive inhibition
4. Non-competitive inhibition
Allosteric regulation