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Enzymes - Coggle Diagram
Enzymes
Allosteric enzymes and isoenzymes
The binding of the regulatory molecule can either enhance the activity of the enzyme (allosteric activation), or inhibit the activity of the enzyme (allosteric inhibition)
The substrate binding site = the catalytic (C) subunits
The modulator binding site = the regulatory (R) subunits
Allosteric and substrate binding sites may or may not
be physically adjacent
Active site: Substrate
Allosteric site: Modifiers/Effecters (Inhibitor or Activator)
Quaternary structure of allosteric enzymes
Tense (T) = Low affinity for substrate
Relaxed (R) = High affinity for substrate
Enzymes with multiple subunits, with each subunit working together (cooperativity)
When the substrate binds to the subunits in the enzyme, this will change the enzyme structure from T to R, allowing other
subunits to bind to the substrate better
Sequential model (Koshland)
Concerted model (Wyman, Momod and Changeux)
Enzymes classification and enzyme nomenclature
Hydrolases
Hydrolysis reactions (transfer of functional groups to water)
Lyases
Addition or removal of groups to form double forms
Transferase
group-transfer reactions
Isomerases
Isomerization reactions (intramolecular group transfer)
Oxidoreductase
oxidation-reduction reactions
Ligases
Ligation of two substrates at the expense of ATP hydrolysis
Factors Affecting Enzyme Activity
Hydrogen ion concentration (pH)
Reaction time
Temperature
Presence of activators and inhibitor
Enzyme concentration
Substrate concentration
Utilization of enzymes in biochemistry
Washing powder, Lipase, Amylase
Bakery industry : Amylase, Prota\ease
Baby food : Trypsin
Rubber industry : Catalase
Enzymes molecular structure
Substrate binding site
Active site or Catalytic site
Allosteric site or Regulatory site
Enzyme kinetics
