Enzyme Structure and Function (BIO, BC) Flashcards
What is the function of enzymes in catalyzing biological reactions?
Enzymes function to lower the activation energy of reactions (do not get used up!)
Enzyme Structure determines function 🡪Thus a change in structure result in a ?
change in function
Enzyme are categorozed by 6 reaction types, list them.
6 Types of Enzymes:
L : Ligase
I : Isomerase
L : Lyase
H : Hydrolase
O : Oxidoreducatase
T : Transferase
What is Ligase Rxn? And What is another name?
Join two large biomolecules, often of the same type.
A + B 🡪 AB
Sometimes joins two molecules through a condensation rxn ( release of H20)
Another name is SyntheTase which means it USES ATP
Example: Carboxylase, Synthetase
What is a Lyase Rxn? Due to the reversal of this rxn, what is another name?
Lyases cleave without the addition of water and without the transfer of electrons. Example : A 🡪 B + C (does not use water, or oxidation/reduction)
HOWEVER, the reverse reaction, synthesis, aka synthase: join two molecules together and don’t need ATP.
A + B –> AB (does not use ATP to join molecules)
Example : Synthase, Decarboxylase
Synthetase vs Synthase
Hydrolases fxn?
Cleavage with the addition of water
Examples : pepsin, amylase, lipase, petidase, nuclease, phosphatase, esterase, glycosylase
A + H2O 🡪 B + C
Isomerase Fxn?
Isomerase is the Interconversion of isomers, including both constitutional and stereoisomers. Examples : Mutase, Epimerase
A 🡪 B
Transferase Fxn?
Move a functional group from one molecule to another
A + BX 🡪 AX + B
Example : Kinases, Phosphorylase
Oxidoreductase Fxn?
Catalyze oxidation-reduction reactions that involve the transfer of electrons
Oxidase = oxidizing or taking away electrons from a molecule
Reductase = reducing or giving electrons to a molecule
A + B: 🡨🡪 A: + B
Examples : Dehydrogenase, Oxidase, Peroixdase
Reduction of activation energy needed for what? & achieved by?
Enzymes lower the activation energy of the reaction (making it easier for the reactants to transition to form products)
Acid/Base catalysis = enzymes use acidic/basic properties to make rxns go faster by proton transfer
Covalent catalysis = enzymes covalently bind to help with electron transfer
Electrostatic catalysis = charged molecules or metal ions used to stabilize big positive or negative charges
Proximity/Orientation effects = enzymes make collisions between reacting molecules happen more often
Transition state = highest energy point from path A to B (in A🡪 B)
Where you also find most instability (high energy = more unstable)
How did Induced Fit Model get it’s name?
Called the induced fit because both the enzyme and substrate have changed their shape a little so they bind together really tightly (catalyzing reaction at full force)
Binding between reactant and enzyme STRONGEST at which state?
Binding between reactant and enzyme STRONGEST at the transition state
Cofactors & Mechanism of catalysis
Directly involved in the enzyme’s catalytic mechanism (might be stabilizing the substrates, or helping the reaction to convert substrates from one form to another) (e.g. Mg2+)
Coenzymes & Mechanism for Catalysis
Organic carrier molecules (i.e. NADH, CoA)