functional enzyme together with its cofactors is called: loenzyme poenzyme oenzyme ostheric enzyme ith regards to the Michaelis-Menten equation, a molecule that has the effect of increasing the nax of a reaction upon binding to an enzyme would be called what? tivator competitive inhibitor n-competitive inhibitor mpetitive inhibitor nich statement is true of enzymes? zymes work independent of substrate concentration. e activity of an enzyme might change as pH changes. anges in temperature do not affect enzymes. zymes catalyze chemical reactions by increasing the activation energy. at is true of an uncompetitive inhibitor? inds only to the complex formed between the enzyme and the substrate educes the activity of the enzyme and binds equally well to the enzyme whether or not it has eady bound the substrate orms the same products as the substrate. inds to the active site of the enzyme. lat is true of a competitive inhibitor? as a structure similar to the substrate. as the same mass as the substrate. orms the same products as the substrate. inds with the enzyme in a place other than the active site of the enzyme. w would a fever most likely affect the activity of enzymes in human body? rould cause the enzyme to adapt to the new temperature. ould slow or stop enzyme function. ill change the amino acid sequence of the enzyme. ould increase enzyme activity. at will happen with the amount of the enzyme after biochemical reaction: amount of the enzyme will always reduce e amount of the enzyme will never reduce e amount of the enzyme will reduce in catabolic reactions e amount of the enzyme will reduce in anabolic reactions te down and explain Michaelis-Menten equation

Question

functional enzyme together with its cofactors is called: loenzyme poenzyme oenzyme ostheric enzyme ith regards to the Michaelis-Menten equation, a molecule that has the effect of increasing the nax of a reaction upon binding to an enzyme would be called what? tivator competitive inhibitor n-competitive inhibitor mpetitive inhibitor nich statement is true of enzymes? zymes work independent of substrate concentration. e activity of an enzyme might change as pH changes. anges in temperature do not affect enzymes. zymes catalyze chemical reactions by increasing the activation energy. at is true of an uncompetitive inhibitor? inds only to the complex formed between the enzyme and the substrate educes the activity of the enzyme and binds equally well to the enzyme whether or not it has eady bound the substrate orms the same products as the substrate. inds to the active site of the enzyme. lat is true of a competitive inhibitor? as a structure similar to the substrate. as the same mass as the substrate. orms the same products as the substrate. inds with the enzyme in a place other than the active site of the enzyme. w would a fever most likely affect the activity of enzymes in human body? rould cause the enzyme to adapt to the new temperature. ould slow or stop enzyme function. ill change the amino acid sequence of the enzyme. ould increase enzyme activity. at will happen with the amount of the enzyme after biochemical reaction: amount of the enzyme will always reduce e amount of the enzyme will never reduce e amount of the enzyme will reduce in catabolic reactions e amount of the enzyme will reduce in anabolic reactions te down and explain Michaelis-Menten equation

Answer 1

1. The correct answer is: oenzyme.2. The correct answer is: activator.3. The correct answer is: The activity of an enzyme might change as pH changes.4. The correct answer is: Binds only to the formed enzyme-substrate complex.5. The correct answer is: Has a structure similar to the substrate.6. The correct answer is: Would slow or stop enzyme function.7. The correct answer is: The amount of the enzyme will reduce in catabolic reactions.8. The Michaelis-Menten equation is a mathematical model that describes the rate of an enzyme-catalyzed reaction as a function of the concentration of the substrate. It is given by the equation:V = (Vmax * [S]) / (Km + [S])Where:V = the initial velocity of the reactionVmax = the maximum velocity of the reaction[S] = the concentration of the substrateKm = the Michaelis constant, which is the substrate concentration at which the reaction velocity is half of Vmax.The equation shows that the reaction velocity increases as the substrate concentration increases, but the rate of increase slows down as the substrate concentration approaches the Km value. When the substrate concentration is much higher than the Km, the reaction velocity approaches Vmax.

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