Only five general types of reactions are commonly observed in biochemical transformations. Given the proposed mechanism (illustrated above) for Class A β-lactamases, what is the biochemical reaction type represented by steps 1 and 2?
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Only five general types of reactions are commonly observed in biochemical transformations. Given the proposed mechanism (illustrated above) for Class A β-lactamases, what is the biochemical reaction type represented by steps 1 and 2?
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- Regulation of Glutamine Synthetase by Covalent Modification Suppose at certain specific metabolite concentrations in vivo the cyclic cascade regulating E. coli glutamine synthetase has reached a dynamic equilibrium where the average state of GS adenylylation is poised atn=6. Predict what change in nwill occur if: [ ATP ] increases, PIIA/PIID increases, [ -KG ]/[ Gln ] increases, [ Pi ] decreases.RuBP carboxylase is not an idel enzyme by any means. Describe some of the active site's and substrate specificity's issues. When the amino acid sequences of this enzyme from several species are compared, they are nearly similar. What importance does this homogeneity have?Lysozyme’s use of aspartic acid and glutamic acid, to break the glycosidic bonds of the eubacterial cell wall (composed of peptidoglycan), illustrates the common enzymatic pattern of: hydrolysis (catabolic), using nonpolar amino acids at the active site hydrolysis (catabolic), using polar amino acids at the active site condensation (anabolic), using nonpolar amino acids at the active site condensation (anabolic), using polar amino acids at the active site all of the above
- The rate of the peptidyl transferase reaction increases as the pH increasesfrom 6 to 8. Explain these results in terms of its reaction mechanism.Many enzymes function best within narrow temperature and pH ranges. Catalase, however, is active over a broad range of temperatures and pH. Explain how this might correlate with the widespread presence of catalase among organisms.biosynthesis of Thymidine monophosphate from ATP, HCO3-, Gln, Asp, quinone, and methylene THF. Show your work and don’t forget that the conversion of U to T only happens AFTER Ribonucleotide Reductase processes the 2’, 3’ ribose to the 3’ deoxy ribose
- RuBP carboxylaseis by no means an idesl enzyme. Describe some of the problems with its active site and its substrate specificity. If we compare the amino acid sequences of this enzyme from many different species, they are almost identical. What is the significance of this uniformity?The enzymatic activity of lysozyme is optimal at pH 5.2 and decreases above and below this pH value. Lysozyme contains two amino acid residues in the active site essential for catalysis: Glu35 and Asp52. The pK value for the carboxyl side chains of these two residues are 5.9 and 4.5 respectively. What is the ionization state of each residue at the pH optimum of lysozyme? How can the ionization states of these 2 amino acid residues explain the pH-activity profile of lysozyme?The enzyme lysozome catalysis the hydrolysis of polymer that consists of N-acetylglucosamine and N-acetylmuramic. This reaction usually takes place at ph=5 but is dramatically inactive above ph=7. Explain why this occurs referring to the catalytic mechanism of lysozome
- Using the ActiveModel for aldose reductase, describe the structure of the TIM barrel motif and the structure and location of the active site.Allosteric Regulation of Purine and Pyrimidine Biosynthesis Illustrate the key points of regulation in (a) the biosynthesis of IMP, AMP, and GMP; (b) E. coli pyrimidine biosynthesis; and (c) mammalian pyrimidine biosynthesis.Distinguishing the Mechanisms of Class I and Class I Aldolases Fructose bisphosphate aldolase in animal muscle is a class 1 aldolase, which forms a Schiff base intermediate between substrate (for example. fructose-1, 6-bisphosphate or dihydroxyacetone phosphate) and a lysine at the active site (see Figure I8.12). The chemical evidence for this intermediate conies from studies with aldolase and the reducing agent sodium borohydride, NaBH4. Incubation of the enzyme with dihydroxyacetone phosphate and NaBH4 inactivates the enzyme. Interestingly, no inactivation is observed if NabH4 is added to the enzyme in the absence of substrate. Write a mechanism that explains these observations and provides evidence for the formation of a Schiff base intermediate in the aldolase reaction.