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CHEM 153A - MT 2 EXAM QUESTIONS WITH CORRECT ANSWERS LATEST UPDATE 2025/2026

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CHEM 153A - MT 2 EXAM QUESTIONS WITH CORRECT ANSWERS LATEST UPDATE 2025/2026 compartmentalization - Answers the separation/concentration of bio-components in specified subcellular sections catalyst - Answers reduces activation energy and thus allows for reactants to get over a (lower) energy barrier cofactors - Answers non-protein components necessary for the reaction EX: metal ions transition state analogs - Answers molecules that mimic the TS but are non-reactive -- bind to enzyme active sites and act as inhibitors oxidoreductases - Answers transfer of electrons, changes oxidation state of atom transferases - Answers transfer of functional group from one molecule to another hydrolases - Answers breakdown of substrate into 2 products using water hydrolysis and condensation rxn (reverse) *requires H2O lyases - Answers removal of a group to form a double bond able to split molecules w/ and w/o H2O ligases - Answers forms one product from 2 substrates coupling with ATP cleavage isomerases - Answers intramolecular rearrangement (isomerization) within a single molecule proximity - Answers crowd substrates into a small active site, significantly speeding up the resulting rxn (when there are 2+ substrates) orientation - Answers enzymes have active sites that optimize the orientation of the reacting molecules relative to each other acid catalysis - Answers the donation (letting go) of a proton (by a residue in the active site), which stabilizes the leaving group base catalysis - Answers the removal of a proton (by a residue in the active site) which can increase the nucleophillicity of a functional group electrostatic catalysis - Answers ANY (not just charged) residues stabilizing the transition state of a rxn through IMFs turnover number (kcat) - Answers the maximal # of substrates converted to product per second for a single enzyme (specifically single active site) Km - Answers the degree of attraction of the substrate to the active site catalytic efficiency - Answers measure of enzyme efficiency (how able the enzyme is to take substrate and produce product quickly) lineweaver-burke plot - Answers graphical representation of enzyme kinetics inverse of the equation derived through MM kinetics RNase A - Answers non-specific enzyme that cuts RNA at any phosphate to 5'-OH bond *following a pyrimidine* proteases - Answers break down proteins by cleaving peptide bonds catalytic triad - Answers system in enzymes where three residues that work cooperatively to effect a nucleophilic attack

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CHEM 153A
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CHEM 153A

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CHEM 153A - MT 2 EXAM QUESTIONS WITH CORRECT ANSWERS LATEST UPDATE
2025/2026

compartmentalization - Answers the separation/concentration of bio-components in specified
subcellular sections

catalyst - Answers reduces activation energy and thus allows for reactants to get over a (lower)
energy barrier

cofactors - Answers non-protein components necessary for the reaction



EX: metal ions

transition state analogs - Answers molecules that mimic the TS but are non-reactive --> bind to
enzyme active sites and act as inhibitors

oxidoreductases - Answers transfer of electrons, changes oxidation state of atom

transferases - Answers transfer of functional group from one molecule to another

hydrolases - Answers breakdown of substrate into 2 products using water



hydrolysis and condensation rxn (reverse)

*requires H2O

lyases - Answers removal of a group to form a double bond



able to split molecules w/ and w/o H2O

ligases - Answers forms one product from 2 substrates



coupling with ATP cleavage

isomerases - Answers intramolecular rearrangement (isomerization) within a single molecule

proximity - Answers crowd substrates into a small active site, significantly speeding up the
resulting rxn

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CHEM 153A
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CHEM 153A

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