Explain the basis for the following statement. For efficient conver- sion of galactose to glucose-1-phosphate, UDP-glucose need be present in catalytic amounts only.
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UDP : Uridine diphosphate glucose is a nucleotide sugar. It is involved in glycosyltransferase reactions in metabolism.
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- The Reactions and Meehanisms of the Leloir Pathway Write the reactions that permit galactose to be utilized in glycolysis. Write a suitable mechanism, tor one of these reactions.Using the ActiveModel for aldose reductase, describe the structure of the TIM barrel motif and the structure and location of the active site.If phenylalanine was not an essential amino acid, would diet therapy (the elimination of phenylalanine from the diet) for PKU work?
- Examine the ActiveModel for alcohol dehydrogenase and describe the structure and function of the catalytic zinc center.Write a balanced equation for each of the following reactions or reaction sequences. (a) The reaction catalyzed by PFK-2 (b) The conversion of 2 moles of oxaloacetate to glucose (c) The conversion of glucose to UDP-Glc (d) The conversion of 2 moles of glycerol toglucose (e) The conversion of 2 moles of malate to glucose-6-phosphateThe cleavage of fructose-1,6-bisphosphate to glyceraldehyde3-phosphate and dihydroxyacetone phosphate is an exampleof an __________________ reaction
- Write a balanced equation for the synthesis of TMP from dUMP that is coupled to the conversion of serine into glycine.Propose a mechanism for the conversion of glucose 6-phosphate into fructose 6- phosphate by phosphoglucose isomerase based on the mechanism of triose phosphate isomerase.A glycolytic intermediate may be used to make the glycerol 3-phosphate necessary for the production of glycerophospholipids. For this conversion, provide a reaction sequence.
- In the first step of the aldolase reaction, an active site Lys229 residue, with its side chain amino group in the deprotonated state, acts as a nucleophile and attacks the carbonyl C2 carbon of fructose 1,6-bisphosphate to form a Schiff base (boxed in the scheme). Since the pKa of the Lys side chain amino group in free solution is ~10.5, the pKa of Lys229 side chain must have been perturbed to a (higher lower) value for the enzyme to be active at neutral pH. the answer should include sufficient details, including the definition of pKa.Identify the enzyme that carry out the below reaction and denotes the nature of the enzyme? UDP-galactose + N-acetylglucosamine ~ UDP + N-acetyllactosamineThe active site of an enzyme that uses a general acid-base catalytic mechanism contains a Glu and an Asp residue (both of which are essential for catalysis) with pKa values of 5.9 and 4.5, respectively. If the enzyme is found in the lysosome (pH = 5.2), which residue will act as the general acid and which will act as the general base during the initial steps of the reaction?
