Amylose n + Water   →   Amylosen-1   +   Glucose  (See attached image of chemical reaction for the above) 1) If amylose and amylase are left together in solution in a test tube for a long period of time, what will be left in the test tube at the end?  2) In an experiment

Determine whether the following reactions will be spontaneous under standard biochemical conditions. Include calculations for Delta G in your answer. Use Table 13-7 in your textbook to help you.a) 2NADH + 2H+ + O2 --> 2NAD+ + 2H2Ob) Malate + FAD --> Oxaloacetate + FADH2c) Pyruvate + H2S --> Lactate + S

The KM values for the reaction of chymotrypsin with two different substrates are given in the table below. Considering this information, which substrate has the lower apparent affinity for the enzyme? Which substrate is likely to give a lower value for Vmax? Substrate N-acetylvaline ethyl ester N-acetyltyrosine ethyl ester KM (M) 8.8 X 10-² 6.6 X 10-4 N-acetylvaline ethyl ester has the lower apparent affinity for the enzyme; it will also likely to give a lower Vmax: N-acetyltyrosine ethyl ester has the lower apparent affinity for the enzyme; it will also likely to give the lower V₁ max. N-acetylvaline ethyl ester has the lower apparent affinity for the enzyme; N- acetyltyrosine ethyl ester is likely to give the lower Vmax: N-acetyltyrosine ethyl ester has the lower apparent affinity for the enzyme; N- acetylvaline will likely to give the lower Vmax. None of the above statements are correct.

Two reactions are shown below. These reactions are directly coupled in cells by an enzyme called hexokinase, which is a key enzyme in glycolysis. It is generally the case that reactions that are directly coupled by enzymes share some common reactants. What is the net reaction when these two reactions are combined? Glucose + Inorganic Phosphate + ATP + Water → Glucose 6-phosphate + ADP Glucose + ATP + Water → Glucose 6-phosphate + ADP + Inorganic Phosphate Glucose + ATP → Glucose 6-phosphate + Inorganic Phosphate Glucose + ATP → Glucose 6-phosphate + ADP

This is a picture of the catalysis of alcohol by ADH with an inhibitor binding as an aldehyde analog. I have two questions. First, what would the enzyme be classified as and why? Also, what would the steps of this mechanism be?

The pKa for histidine is pKa = 6.1 while that for cysteine is pKa = 8.0 2. Assume that both histidine and cysteine are catalytic groups for a particular enzyme. Assume also that the side chain of cysteine must be in the deprotonated form. Estimate the pH at which the catalytic activity of this enzyme is the maximum and sketch a pH-activity graph.

Consider the following chemical equation whose delta(G) = 9kcal/mol: AC + BD ---> AB + CD    what are the reactants and what are the products  is this reaction spontaneous? How do you know?  Is energy released or consumed by this reaction?  If an enzyme, which catalyzes this reaction is added, what will happen to delta (G) If this reaction is coupled to another reaction, whose delta(G) is -12 kcal/mol, what will be the net delta(G) value? will the overall reaction be spontaneous

Can you please help solve this problem?

Given the tri-acylglyceride (TAG) below as source of energy when administered from an organism's diet, H,C-O HC-0 H,C-o [A] Show the calculated maximum amount of ATP that could be generated by the full oxidation of the compound. Illustrate where the ATPS are derived from (show the reactions and enzymes involved). You can use general structure of the FFA in the reactions involved in the process. (B) Discuss the fate of the glycerol. (C] One of the FFAS derived from the TAG has the same carbon number as glucose. Compare the maximum yield of ATP derivable from this FFA as compared to the ATP yield from glucose.

Write the balanced reaction catalyzed by phophoenolpyruvate carboxylase (P PC). Remember to add any cofactors, and to draw the structure formulas (a line-bond representation is fine) for the main substrate and product of the reaction.