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Enzyme catalyst for biochemical reaction. For each cell a huge number of enzyme exists to
catalyze each reaction. Unlike inorganic catalysts enzymes are moderated to the proper needs of
the body.
Enzymes where discovered in 19th century Germany. They are proteins and therefor have a
complicated structure.
Molecule
Primary, secondary and tertiary structure. Some enzymes are monomeric (one polypeptide) and
some polymeric. Large biopolymers of a large molecular weight. Enzymes can be only simple
or conjugated proteins. Ions like copper. Iron are present in metaloenzymes which are
conjugated enzymes. Most common are organic enzymes in which cofactors of small organic
molecules and metallic ions are present and they are called coenzymes. Apoenzyme + co
enzymes = holoenzymes.
Reactant > progress of reaction > product
If enzyme is not present a significant amount of activation energy has to be used for example
lighting a match requires high friction. The enzyme does not change. Enzymes are able to
modify reaction rate.
Active side
Some parts of the enzymes are responsible of the catalytic effect active side, in which specific
chemical composition for substrate. The shape of the active site must be similar to the shape of
substrate, secondary interaction in inactive part changes the shape of the substrate to fit active
side. Active side insures optimal orientation of reactants. Electrostatic interactions, charged
groups causes faster reactions. Acidbase catalysis. Covalent catalysis causes normal covalent
bonds to occur.
Coenzymes can vary in position and strength of connection to enzyme.
In 1916 a systematic naming for enzymes was introduced. Ending ase according of substrate
name or name of reaction.
Isoenzymes
Some subunits are not the same in primary structure. A group of enzymes with the same activity
but different struction are called isoenzymes. In Lactodihydroginase two types of chains M, H
are present in different combinations in tertiary enzyme (H3M, M3H. M2H2, M4. H4).
Allostremic effect
Only possible in tertiary structure. Allostremic effector molecule which bind to surface of sub
unit changing shape to open (positive effector) or close (negative effectors) active side.
Individual metabolic products can serve as activators inhibitors of allostremic enzymes. They are
known as regulatory enzymes. If ATP production is very high, some enzymes serve as negative
effectors to stop production.
Enzymatic activity
Enzyme amount is not a good way to measure activity.
A unit for measurement of activity during time. Turnover number Number of molecules of
substrate changed by one molecules of enzyme per second. kat activity that changes 1 mole of
substrate per second. 1 C activity that changes 1 milimole per minute.
Proteosynthesis machinery produces proenzymes (nonstable) like pepsin synthesizes as
pepsinegin not fully synthesized. These enzymes start partial activation but only the final
enzyme is fully active.
Inhibition of enzymes
Stopping of effect of enzymes. Could be reversible or irreversible. Reversible could be
competitive inhibitor competes with substrate for binding to active side. Uncompetitive binds
only to ES distinct from active side. Uncompetitive binds to both free enzyme and ES distinct
from active side.
Irreversible can be affinity labels highly reactive substrate block active side. Mechanism based
inhibitors substrate
Enzyme modification
• pH (pH optimum) controls dissociation rate of parts of the enzymes.
• Temperature (temperatureoptimum)
• Ionic strength (salt concentration) can remove hydration field and cause changing of
shape
• Others (presence of emulgators lipases)
• Product inhibition (accumulation of product decreases the reaction rate)
• Covalent modification
Phosphorylation
Adenhylation
Uridylation
Ribozylation
Methylation
Proteolytic
Others (metal complex formatiom, disulfidic bond disruption)
• Allosteric modification
Allostreic effectors (Hormones) activators, inhibitors
Feedback inhibition inhibition of former enzymes.
Classification of enzymes
Each cell has more than 3000 enzymes. Each species has a different set of enzymes. There are 6
classes of enzymes.
1. Oxidoreductases oxid reduction reactions
2. Transferases group transfer only group without noncoenzymes
3. Hydrolases Hydrolytic reaction
4. Lyases elimination of groups addition of energy
5. Isomerases reaction involving isomerization (intramolecular changing of groups)
6. Ligases Two molecules joining together requires additional energy from ATP