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Enzymes
Proteins that accelerate, regulate, and coordinate chemical reactions in biological systems.
Vitalism
The belief that living organisms are fundamentally different from inanimate objects due to the presence of a non-physical element.
Coenzymes
Complex organic molecules or vitamins required for enzyme activity.
Apoenzyme
The inactive form of an enzyme when it is not bound to its cofactor.
Holoenzyme
The active form of an enzyme when it is bound to its cofactor.
Catalyst
Substance that lowers the activation energy required for a reaction to proceed.
Specificity
The property of enzymes to catalyze a particular reaction without side reactions.
Transition State
The high-energy state during a reaction where substrates are converted into products.
Michaelis-Menten Kinetics
A model that describes the rate of enzyme-catalyzed reactions with substrate concentration.
kcat
Turnover number; the number of substrate molecules converted to product per enzyme molecule per unit time under saturating conditions.
Allosteric Regulation
The regulation of enzyme activity through binding of molecules at sites other than the active site.
Endergonic Reaction
A reaction that requires an input of free energy to occur.
Exergonic Reaction
A spontaneous reaction that releases free energy.
Serine Proteases
Digestive enzymes that cleave peptide bonds in proteins, activated as zymogens.
Enzyme Inhibition
The process by which an inhibitor molecule decreases or eliminates the activity of an enzyme.
Covalent Modification
The attachment of a modifying group to a protein, affecting its activity.
Glycogen Synthase
An enzyme that produces glycogen from glucose.
Glycogen Phosphorylase
An enzyme that breaks down glycogen into glucose.
Cooperative Activation
A phenomenon where binding of a substrate enhances the activity of an enzyme.
Serine Residues
Amino acids that often play a role in the catalytic mechanism of enzymes.
Substrate Concentration (S)
The amount of substrate available for enzyme reactions, impacting the rate of reaction.