[Glucose Phosphate]453525155Glucose-phosphate production atfour blood sugar levels10[0.25] and [0.40][0.10]units.[0.05]9050Time in secondsGlucose-phosphate production by an enzyme extracted from cells taken from the much-fearedLilyputin in media with four different glucose levels is provided above. The fasting blood sugarlevels of this animal fall between 0.40 and 0.60 sugar units.The enzyme catalyzing this reaction must beenzyme was extracted could have beencells (enter one of these choices).The Km of this enzyme to three decimal places isand the cells from which themuscle cells /pancreatic betaEnter only a number, no

Hexokinase catalyze the conversion (phosphorylation) of Glucose to Glucose 6 phosphate (mentioned as…

Answered: [Glucose Phosphate] 45 35 15…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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Calculcate Kcat for PNP substrate for both enzyme concentrations. enzyme volume: 20 ul Bovine Intensince Alkaline phosphatase molecular weight: 140,000 Bovine intenstine Alkaline phosphatase activity: 300 units/ml and 14 units/mg extinction coefficient PNP: 18.5 abs (mM-1 cm-1) Vmax: 0.332 moles/sec a) enzyme 1 concentration: undiluted b) enzyme 2 concentration: 1:1 dilution
PRESSURE OF A WHAT IS THE asmoTIC SOLUTION OF BOVINE insuLIN (MOLAR MASS, 5700g mol - 1 ) aT 18 °C IF 100.0 ML OF THE SOLUTION conTains 0.103 a OF THE INSULIN?
is this stement false? Intracellular concentrations in resting muscle are as follows: Fructose-6-phosphate (1.0 mM)Fructose-(1-6)-bisphosphate (10.0 mM)AMP (0.1 mM)ADP (0.5 mM)ATP (5.0 mM)Pi (10.0 mM)Under the above conditions the Phosphofructokinase reaction in muscle is more exergonic than under standard conditions.
The following initial-rate data were obtained on the rate of binding of glucose w ith the enzyme hexokinase (obtained from yeast) present at a concentration of 1.34 mmol dm-3. What is (a) the order of reaction with respect to glucose. (b) the rate constant?[C6H12O6]/(mmol dm-3) 1.00 1.54 3.12 4.02vo/(mol dm-3 s-1) 5.0 7.6 15.5 20.0
The inilial reactions in the biosynthesis of the amino acid aspartate at 298 K are: Carbamoyphoephate Cartamoyi + phosphate ADP + phoaphate - ATP AO=-12,300 calmol AG-T800 calimol Which of the following statements is gorrect? A) The energy which is released fron the conversion of 1 mole of carbamoyphosphate to carbamoyl+ phosphate (P) in reaction I is sufficient to drive the synthesis of 1 mole of ATP in reaction II. B) AG for the reaction Carbamoyphosphate + Carbamoyl + phosphate is +123 kcalimol. c) AHP for reaction I cannot be detemined trom the information given. D) Al of the above. E) None of the above.
The enzyme serine hydroxymethy ltransferase (SHMT) catalyses the conversion of serine into glycine. The fo llowing table gives the initial rates, vo, for the SHMT-catalysed reaction of the substrate serine at var ious concentratio ns of serine, lSI.[S]/(mmol dm-3) 10 20 30 40vo(μmol dm-3 s-1) 1.63 2.94 4.10 4.95Use the data to determine the values of the MichaelisMenten constant, the maximum velocity of the reaction, and the maximum turnover number of the enzyme.
The standard free energy change for this reaction in the direction written is +23.8 kuimol. The tabie shows the concentrations of the three intermediates in the hepatocyte of a mammal. Intermediate Concentration (M) Fructose 1.0-bisphosphate 0.000028 Gyoeraldehyde 3phosphate 0.0000068 Ditydroxyacetone phosphate 0.000032 At body temperature (37 "C). what is the actual free energy change for the reaction (in kimol) ?
TABLE 3-LACTATE PRODUCTION IN FORTIFIED HEMOLYSATES OF HUMAN ERYTHROCYTES* Substrate Glucose Glucose Lactate production† No. of experiments pH 6 7.1 2.03 ± 0.91 6 7.8 4.76 ± 1.09 7-1 10-73 +1-88 5 7.8 12.34 ±2.92 5 7.0 7-15±0.73 5 7-7 (b)( ) In mature erythrocytes (red blood cells) the end product of glycolysis is lactate because of the absence of mitochondria. On the right is a table comparing the rate of lac- tate production in hemolysates (lysed cells) of human RBCs as a function of pH with dif- ferent substrates introduced into the glyco- lytic pathway. The hemolysate was fortified with 30 μmoles substrate, 7.5 μmoles MgCl2, 10 μmoles disodium phosphate, 1.5 μmoles NAD and 5 μmoles ATP in a volume of 5 mL. The rate of lactate production is given as μmoles of lactate/g Hb/hr at 37° C, buffered to either pH 7.1 or 7.8, as indicated. According to the results in the table which glycolytic enzyme is rate-limiting? Explain. Glucose-6-phosphate Glucose-6-phosphate Fructose-1,6-diphosphate…
Calculate the free energy change for glucose entry into cells when the extracellular concentration is 4.5 mM and the intracellular concentration is 2.1 mM at 37oC. Express your answer in kJ/mol.
In glucose estimation using Benedict's Reagent, what is/are the chemical reaction/s that resulted in the white precipitate observed.
A new drug, Proinebrium, that reduces Kcat (Ki = 2.0 uM) has been developed to treat ethylene glycol poisoning. (1) What concentration of Proinebrium is required to achieve 50% inhibition of ethylene glycol metabolism by alcohol dehydrogenase when the concentraion of ethlyene glycol in the blood is 50 uM?
these are KT values. Which transporter that is a GLUT will transport glucose from blood which is 5nm at the maximum or Vmax? Is it (GLUT 11,KT= 0.1M), (is it GLUT1, KT = 3nm), (is it GLUT 2, KT= 17nm), (or GLUT 4, KT = 5nm)

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