From the complete oxidation of glucose (glucose → 6CO2), how many total nucleotide triphosphates are yielded (be sure to deduct payback) as part of substrate level phosphorylation?
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- Using the ActiveModel for aldose reductase, describe the structure of the TIM barrel motif and the structure and location of the active site.Figure 27.3 illustrates the response of R (ATP-regenerating) and U (ATP-utilizing) enzymes to energy charge. a. Would hexokinase be an R enzyme or a U enzyme? Would glutamine: PRPP amidotransferase, the second enzyme in purine biosynthesis, be an R enzyme or a U enzyme? b. If energy charge = 0.5: Is the activity of hexokinase high or low? Is ribose-5-P pyrophosphokinase activity high or low? c. If energy charge = 0.95: Is the activity of hexokinase high or low? Is ribose-5-P pyrophosphokinase activity high or low?The Energetic Cost of Nitrogen Excretion via the Urea Cycle How many ATP equivalents are consumed in the production of 1 equivalent of urea by the urea cycle?
- From the complete oxidation of glucose (glucose → 6CO2), how many total nucleotide triphosphates are yielded (be sure to deduct payback) as part of substrate level phosphorylation?Consider the complete oxidation of one mole of simple TAG containing behenic acid residues (22:0). I. For one mole of the fatty acid residue, determine the following: c. What is the number of ATP yield obtained from FADH2 coming from the complete β-oxidation of the fatty acid residueHexokinase is an important enzyme in the metabolism of glucose. If theconcentration of hexokinase in our eukaryotic cell is 20 μM, how many glucose molecules are present per hexokinase molecule?
- Using the word anomeric carbon, “acceptor” nucleophilic substrate, and activated “donor”, describe how Glycosyl transferase's (and glycosidases) catalyze glycan and glycoconjugate formationWhat is the smallest number of molecules of ATP and GTP consumed in the synthesis of a 200- residue protein, starting from amino acids? Assume that the hydrolysis of PP i is equivalent to the hydrolysis of ATP for this calculation.The uncatalyzed reaction rate for the conversion of substrate X to product Y is one year. The enzyme-catalyzedrate is one millisecond. Describe the features of theenzyme that are probably responsible for this ratedifference.
- a) Write the catalytic mechanistic steps used in the urea cycle. If transamination is required, showonly the net reaction of this step.b) Where do the 2 nitrogen atoms and the 1 carbon atom that make the final product come from?The M and H subunits of lactate dehydrogenase have very similar sizes and shapes but differ in amino acidcomposition. If the only difference between the two were that theH subunit had a glutamic acid in a position where the M subunithad a serine, how would the five isozymes of LDH separate on electrophoresis using a gel at pH 8.6?The sedimentation value of aspartate transcarbamoylase decreases when the enzyme switches to the R state. On the basis of the allosteric properties of the enzyme, explain why the sedimentation value decreases.