the slowest reaction in a sequence is the - ANSWER rate-limiting step
the state of a system in which no further net change is occurring - ANSWER
equilibrium
the assumption that the rate of formation of ES is exactly equal to the rate of
breakdown of ES is called the _____ _____ assumption - ANSWER steady
state
K cat is known as the _____ number. at saturating substrate concentrations,
kcat=vmax/[Et] - ANSWER turnover number
type of inhibitor that alters the Km of an enzyme without altering vmax -
ANSWER competitive
molecule that binds to the active sit of an enzyme - ANSWER substrate
Relatively small portion of an enzyme that is involved in substrate binding -
ANSWER active site
Describes changes in the conformation of an enzyme upon substrate binding -
ANSWER induced fit
, A ____-_____ analog binds more tightly to the active sit than does the substrate
molecule - ANSWER transition state
______-______ kinetics describes the enzymatic activity of an idealized
enzyme - ANSWER Michaelis menten
Trypsin is to trypsinogen as active enzyme is to - ANSWER zymogen
Complete enzyme complex containing all the protein subunits and prosthetic
groups - ANSWER holoenzyme
Type of energy obtained from the interaction of enzyme and substrate that
decreases the activation energy for a reaction - ANSWER binding
A binding site of a protein is structurally complementary to a specific ligand
because of what characteristic of the binding site? - ANSWER Size
Shape
Charge
Hydrophobicity
Which of the following molecules is bound MOST strongly to the heme iron? -
ANS CO
Which amino acid in hemoglobin is a ligand to iron in addition to the heme
prosthetic group? - ANS Histamine
Hemoglobin participates in the transportation of which ion and/or molecule in
the blood? - ANS CO2, O2, and H+
the state of a system in which no further net change is occurring - ANSWER
equilibrium
the assumption that the rate of formation of ES is exactly equal to the rate of
breakdown of ES is called the _____ _____ assumption - ANSWER steady
state
K cat is known as the _____ number. at saturating substrate concentrations,
kcat=vmax/[Et] - ANSWER turnover number
type of inhibitor that alters the Km of an enzyme without altering vmax -
ANSWER competitive
molecule that binds to the active sit of an enzyme - ANSWER substrate
Relatively small portion of an enzyme that is involved in substrate binding -
ANSWER active site
Describes changes in the conformation of an enzyme upon substrate binding -
ANSWER induced fit
, A ____-_____ analog binds more tightly to the active sit than does the substrate
molecule - ANSWER transition state
______-______ kinetics describes the enzymatic activity of an idealized
enzyme - ANSWER Michaelis menten
Trypsin is to trypsinogen as active enzyme is to - ANSWER zymogen
Complete enzyme complex containing all the protein subunits and prosthetic
groups - ANSWER holoenzyme
Type of energy obtained from the interaction of enzyme and substrate that
decreases the activation energy for a reaction - ANSWER binding
A binding site of a protein is structurally complementary to a specific ligand
because of what characteristic of the binding site? - ANSWER Size
Shape
Charge
Hydrophobicity
Which of the following molecules is bound MOST strongly to the heme iron? -
ANS CO
Which amino acid in hemoglobin is a ligand to iron in addition to the heme
prosthetic group? - ANS Histamine
Hemoglobin participates in the transportation of which ion and/or molecule in
the blood? - ANS CO2, O2, and H+
