For questions 12-13, refer to the following table. Enzyme carbonic anhydrase fumarase ribonuclease 12. 13. acetylcholinesterase KM (mol/L) 2.6 x 10-2 5 x 10-6 Kcat (S-1) 4 x 105 800 7.9 x 10-3 9.5 x 10-5 790 1.4 x 104 (1 point) Calculate the initial reaction velocity for acetylcholinesterase (corresponding to the initial few percent of substrate consumed). Assume a total enzyme concentration of 1 nM and substrate concentration of 100 mM. Show your work. (1 point) For ribonuclease, what concentration of substrate is needed to produce half the velocity that would be obtained in the limit of an "infinitely high" concentration of substrate?

Reaction Velocity (mm/sec) Ma no !! L [1 1 L IM 3M FO Substrate Concentration (M) 1. IN Which statement is true? KM AN ALM 4V The graph above displays the kinetic profiles of the same enzyme catalyzing two different substrates. The red curve displays the higher turnover number (kcat). The red curve displays higher affinity between substrate and enzyme. The blue curve displays competitive inhibition. The red curve displays higher cooperativity,

The above diagram illustrates ___? The relationship between the proteome and the metabolome The relationship between the concentration of enzymes and the rate of chemical reactions they catalyze a and b

The following data were obtained in a study of an enzyme known to follow Michaelis-Menten kinetics. Product formed (mmol/min) Substrate added (mmol/L) 217 0.8 325 2 433 4 488 6 647 1000 The Km for this enzyme is approximately: 4 mM. 2 mM. 1 mM. 6 mM. 1000 mM.

The "hill" in the activation profile that reactants must pass over is called the:

Suppose that, in the absence of a catalyst, a certain biochemical reaction occurs x times per second at normal body temperature 137 °C2. In order to be physiologically useful, the reaction needs to occur 5000 times faster than when it is uncatalyzed. By how many kJ>mol must an enzyme lower the activation energy of the reaction to make it useful?

Please give me very detailed solution.

1. A daily low dosage of aspirin (acetylsalicylic acid) can lower the risk of heart attack and stroke for individuals at risk. Aspirin suppresses the generation of prostaglandins by irreversible binding to the enzyme COX-1. Inhibition of prostaglandin synthesis lowers the production of thromboxanes that are responsible for the aggregation of platelets and the formation of blood clots. You will explore the mechanism of aspirin binding. 1.1 The average pH of the human body is 7.4 (also known as a physiological pH). Draw the structure of aspirin at a physiological pH. OH 1.2 Aspirin reacts with the amino acid Serine. What is the structure of serine? Draw the structure of the tripeptide Ala-Ser-Trp (draw these structures as they exist at physiological pH) serine Ala-Ser-Trp 1.3 Aspirin reacts with Serine 530 of COX-1 by transesterification reaction. Draw a general mechanism of acid-catalyzed transesterification reaction. Use HA as an acid. 1.4 Draw an arrow-pushing mechanism for the…

Q 25 please

Write the Ksp expression for the sparingly soluble compound calcium phosphate, Ca3(PO4)2- Ksp If either the numerator or denominator is 1, please enter 1.