One form of DNA damage, methylation of adenosine residues, destabilizes them. At 37 °C, the tj/2 for residue breakdown decreases from 37 y to 37 min. By how much does the activation energy decrease upon adenosine methylation? (Assume that A is constant.) | 24 kJ/mol ) 7.8 kJ/mol 18 kJ/mol 34 kJ/mol

One form of DNA damage, methylation of adenosine residues, destabilizes them. At 37 °C, the tj/2 for residue breakdown decreases from 37 y to 37 min. By how much does the activation energy decrease upon adenosine methylation? (Assume that A is constant.) | 24 kJ/mol ) 7.8 kJ/mol 18 kJ/mol 34 kJ/mol

Curren'S Math For Meds: Dosages & Sol

11th Edition

ISBN:9781305143531

Author:CURREN

Publisher:CURREN

Chapter9: Parenteral Medication Labels And Dosage Calculation

Section: Chapter Questions

Problem 6.4P

See similar textbooks

Similar questions

Intramitochondrial ATP concentrations are about 5 mM, and phosphate concentration is about 10 mM. If ADP is five times more abundant than AMP,calculate the molar concentrations of ADP and AMP at an energy charge of 0.85. Calculate ∆G for ATP hydrolysis at 37 °C under these conditions.The energy charge is the concentration of ATP plus half the concentration of ADP divided by the total adenine nucleotide concentration.
A particular enzyme has a ΔΔG‡ of -22.1 kJ mol-1 at 37.0 °C. Calculate the rate enhancement of this enzyme. (R = 8.3145 J mol-1 K-1)
Intramitochondrial ATP concentrations are about 5 mM, and phosphate concentration is about 10 mM. If ADP is five times more abundant than AMP, calculate the molar concentrations of ADP and AMP at an energy charge of 0.85. Calculate AG for ATP hydrolysis at 37 °C under these condi- tions. The energy charge is the concentration of ATP plus half the concen- tration of ADP divided by the total adenine nucleotide concentration: [ATP] + 1/2[ADP] [ATP] + [ADP] + [AMP]
Sphingosine-1-phosphate (S1P) is important for cell survival. The synthesis of S1P from sphingosine and ATP is catalyzed by the enzyme sphingosine kinase. An understanding of the kinetics of the sphingosine kinase reaction may be important in the development of drugs to treat cancer. The velocity of the sphingosine kinase reaction was measured in the presence and absence of threo-sphingosine, a stereoisomer of sphingosine that inhibits the enzyme. The results are shown below. Construct a Lineweaver-Burk plot to answer the following questions: (a) What are the apparent KM and Vmax values in the presence and absence of the inhibitor? (b) What kind of an inhibitor is threo-sphingosine? Explain.
Sphingosine-1-phosphate (S1P) is important for cell survival. The synthesis of S1P from sphingosine and ATP is catalyzed by the enzyme sphingosine kinase. An understanding of the kinetics of the sphingosine kinase reaction may be important in the development of drugs to treat cancer. The velocity of the sphingosine kinase reaction was measured in the presence and absence of threo-sphingosine, a stereoisomer of sphingosine that inhibits the enzyme. The results are shown below. Construct a Lineweaver–Burk plot to answer the following questions: (a) What are the apparent KM and Vmax values in the presence and absence of the inhibitor? (b) What kind of an inhibitor is threo-sphingosine? Explain.
A particular reaction has a ΔG‡ of 30.0 kJ mol-1 at 25.0 °C. In the presence of an enzyme, the same reaction has a ΔG‡ of 1.50 kJ mol-1 at the same temperature. Calculate the rate enhancement of this enzyme. (R = 8.3145 J mol-1 K-1)
The isomerization of dihydroxyacetone phosphate (DHAP) to glyceraldehyde 3-phosphate (GAP) is catalyzed by triose phosphate isomerase. In the cell, the concentration ratio of DHAP/GAP = 5.5. Calculate [DHAP] (in M) when [GAP] = 0.00002
The turnover number of the enzyme fumarase that catalyzes the reaction, Fumarate + H20 ===→ L-malate, is 2.5 x 103 S - l and Km = 4.0 X 10- 6 mol/L. Calculate the rate of conversion of fumarate to L-malate if the fumarase concentration is 1.0 x 1 0 - 6 mol/L and the fumarate concentration is 2.04 x 10- 4 mol/L.
Following is a Dixon plot for PNPP inhibition by inorganic phosphates. What answer choice shows the correct combination of the mode of inhibition and Ki of the EI complex? - Mixed inhibition, Ki= -21.2 uM - Mixed inhibition, Ki= 1/16.5 uM - Competitive inhibition, Ki= 16.5 uM - Competitive inhibition , Ki= -1/16.5 uM - None of the above
The ΔG°′ for hydrolytically removing a phosphoryl group from ATP is about twice as large as the ΔG°′ for hydrolytically removing a phosphoryl group from AMP (−14 kJ · mol−1). Explain the discrepancy.
An experiment was carried out to measure the reaction rate of hydrolysis of acetylcholme (substrate) with serum enzymes (Eadie, 1949). In the experiment, two experiments were conducted, namely experiment 1 without using a prostigmine inhibitor and experiment 2 using a prostigmine inhibitor at 1.5 x 10^-7 mol/l. the data obtained are: a. Is prostigmine competitive or noncompetitive inhibitor? b. determine the value of km and rmax for the two experiments, compare
Sphingosine 1-phosphate (SPP) is important for cell survival. The synthesis of SPP from sphingosine and ATP is catalyzed by the enzyme sphingosine kinase. An understanding of the kinetics of the sphingosine kinase reaction may be important in the development of drugs to treat cancer. The velocity of the sphingosine kinase reaction was measured in the presence and absence of threo-sphingosine, a stereoisomer of sphingosine that inhibits the enzyme. The results are shown below .[Sphingosine], μM 2.5 3.5 5 10 20 50 v0(mg·minꟷ1) no inhibitor 32.3 40 50.872 87.7 115.4 v0(mg·minꟷ1)with threo-sphingosine 8.5 11.5 14.6 25.4 43.9 70.8 Construct a Lineweaver-Burk plot to answer the following questions:(A)What are the apparent KMand Vmaxvalues in the presence and absence of the inhibitor?(B)What kind of inhibitor is threo-sphingosine? Explain this type of inhibition.