Consider the metabolic pathway show below that converts substrate A to B with the enzyme A-ase, B to C with B-ase(1), and so forth. Acety/A-ase A-ase Acetate Deacetylase A Protease D & D A-ase B-ase C-ase BC- Inhibition What is the mechanism of regulation of B-ase? Positive allostery Reversible Covalent modification Isoenzymes Proteolytic Activation Feedback Inhibition
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- Consider the metabolic pathway show below that converts substrate A to B with the enzyme A-ase, B to C with B-ase(I), and so forth. Acety/A-ase A-ase Acetate Deacetylase D Protease B-ase C-ase A-ase ABC- What is the mechanism of regulation of B-ase? Positive allostery Reversible Covalent modification Isoenzymes Proteolytic Activation Feedback InhibitionIn serine protease catalytic triad mechanism, the first and second products that leaves the active site are Carboxylic acid and amide respectively Amide and carboxylic acid respectively Ester and amide respectively Carboxylic acid and ester respectivelyShown below is a substrate for a Trypsin. Draw the mechanism for this serine protease using the artificial substrate. Be sure to draw the catalytic triad, and show the role of the oxyanion hole. Draw the complete structure of every intermediate and product and PUSH ARROWS!!!!! Do not abbreviate structures using R and R' H₂N _N_CH. сно CH₂ CH₂ CH₂ NH d=19H₂ NH₂ O CH- H₂C HN O CH
- Shown below is a substrate for a Elastase. CH, HN NH NH, Draw the mechanism for this serine protease using the artificial substrate. Be sure to draw the catalytic triad, and show the role of the oxyanion hole. Draw the complete structure of every intermediate and product and PUSH ARROWS!Trypsin uses a nearly identical mechanism as chymotrypsin (including the catalytic triad his57-ser195-asp102. beginning with the enzyme substrate complex draw the complete steps in the trypsin mechanism that occur to release the first product and create the acyl enzyme intermediate in the trypsin active site. The substrate for trypsin to be used is gly-lys-gly-ala(c) On the right is a diagram of the ac tive site of E. coli aspartate aminotrans- ferase illustrating the cofactor pyridoxal phosphate (labeled PLP) with the dicar- boxylic acid maleate (labeled MAL) bound in the active site. The structural formula of maleate is shown on the right. Am 194 MAL Arg292 Arg386 Ilx17 Lauf 'coo- H get H Coo- Maleate (c1) Draw the structure of L-aspartate and draw a border around the atoms in the amino acid that maleate simulates. (c2) Identify the active site residues that make hydrogen bonds and electrostatic interac- tions with the oxygen atoms of the carboxylate groups of maleate in the diagram above. Identify the carboxylate groups according to the numbering in the diagram of maleate above. Indicate the hydrogen donor groups of the active site residues. (C3) Compare and draw the structures of L-Arg and L-Lys. On the basis of the diagram why does replacement of an arginine for a lysine have an effect on substrate binding to AspAT? (c4) Of the mutant…
- The diagram below shows the substrate binding cleft for a protease, providing the substrate structure, and indicating the residues (using one-letter code) that line the four specificity pockets. 1 M F H₂N K R IZ 2 3 P F S W оо E 4 The protease is known to cleave the amide linkage between W and E residues for substrates containing the WEFD sequence. Using 3-letter code with amino acids linked by a "dash" (ex. GLY-ALA), the N-terminal product is A and the C-terminal product is A6-Mercaptopurine , after its conversion to the corresponding nucleotide through salvage reactions, is a potent competitive inhibitor of IMP in the pathways for AMP and GMP biosynthesis. It is therefore a clinically useful anticancer agent. The chemotherapeutic effectiveness of 6 mercaptopurine is enhanced when it is administered with allopurinol. Explain the mechanism of this enhancement.serine proteases act via a two-step catalytic mechanism. However, as a critical scientist, you may want to see data that supports this claim. One experiment that can provide such evidence is called a 'pre-steady state' kinetics experiment using the chromogenic substrate, N-acetyl- phenylalanine p-nitrophenyl ester. As shown below when this substrate is cleaved, the p-nitrophenylate is a yellow product whose absorbance can be measured in real time using a spectrophotometer. When the chromogenic substrate is rapidly mixed together with a limiting amount of protease enzyme, the accumulation of product is measured right away on fast (millisecond) timescales. In this experiment, one observes two distinct phases of the reaction as shown in the plot below. Based upon what you know about the mechanism of serine proteases, provide a mechanistic interpretation for the observation of these two phases of the reaction. + H₂O N-Acetyl-L-phenylalanine p-nitrophenyl ester p-Nitrophenolate Absorbance…
- ATCase catalyzes the conversion of carbamoyl phosphate and aspartate into N-carbamoylaspartate, a precursor in pyrimidine biosynthesis. What roles do ATP and CTP play in this reaction? uncompetitive inhibitors heterotropic modulators homotropic modulators mixed inhibitorsDescribe a common feature at the active site of serine proteases and acetyl cholinesteraseWhich of the following statements about ribozyme catalytic residues is INCORRECT? General acid catalysis requires the standarde nucleotide exchangeable proton acidities (represented by pKa values). Ribozymes work by lowering the AG‡ through transition state stabilization without changing the overall AG of the reaction. Some ribozymes cleave phosphodiester bonds, and like proteases, can be autocatalytic. There are fewer known classes of mammalian ribozymes than mammalian enzyles.