NH, N. NH NH NH2 Benzamidine and Leupeptin are competitive trypsin inhibitors. They are shown in their deprotonated forms at high pH. Modify the above drawings to show the protonation and charge at pH 7.0 Draw competitive inhibitors for chymotrypsin based on these structures ZI
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- Salicylamides are inhibitors for an enzyme called scytalone dehydratase. SAR shows that there are three important hydrogen bonding interactions. Explain whether you think quinazolines could act as a bioisostere for salicylamides.Homopolysaccharide are found abundant in nature. Explain how this class ofpolysaccharide acts as primary component of plants and insects.The substitution of His 64 of carbonic anhydrase II with Ala results in a sharp decrease in the activity of the enzyme in HEPES buffer (molecular weight of HEPES = 238.3 g/mol). However, increasing concentrations of imidazole (molecular weight = 68.1 g/mol) restores the reaction rate close to that of the wild-type enzyme. Propose an explanation for these results.
- Chymotrypsin information about enzyme? Trivial/Common Name Systematic (EC) name and number Chemical reaction catalyzed Metabolic pathway Function and cellular localization Size (kDa) and structure (tertiary and quaternary) pH stability Kinetic properties (Km- and Kcat value/s for natural substrates) Stability and potential inhibitorsCarboxylic acids, such as the one shown below, can be difficult to reduce Provide the name of a reductant A. Explain why this reductant is able to react with the carboxylic acid whereas others cannot (Hint: Draw and discuss the potential reactive intermediates/transition states).MULTIPLE CHOICE In patients with Lesch Nyhan Syndrome, purine nucleotides are overproduced and over excreted. The hypoxanthine analogue Allopurinol, which effectively treats gout , has no effect on the severe neurological symptoms of Lesch- Nyhan patients because it does not A. decrease de novo pyrimidine synthesis B. decrease de novo purine synthesis C. decrease urate synthesis D. increase PRPP levels (Phosphoribosyl pyrophosphate)
- A competitive inhibitor interacts with the free enzyme to form an enzyme•inhibitor complex(E•I). This equilibrium reaction can be described as follows:E + I ⇌ EIModify the simplified kinetic scheme for the reaction E + S ⇌ E + P to include this equilibriumexpressionThere are parts A-C for this picture included. A) What type of enzyme is Malate Dehydrogenase? choices: Hydrolase, Isomerase, Ligase, Oxideoreductase, Transferase, or Translocase B) Which of the following statements are true in biochemical standard conditions? There can be more than 1. Choices: The reaction is spontaneous since ∆G°' is positive The reaction is spontaneous since ∆G°' is negative The reaction is not spontaneous since ∆G°' is positive The reaction is not spontaneous since ∆G°' is positive The equilibrium favors products since K is greater than 1 The equilibrium favors reactants since K is greater than 1 The equilibrium favors products since K is less than 1 The equilibrium favors reactants since K is less than 1 The reaction is always at equilibrium C) If the concentration of Oxaloacetate is 10^7 times lower than the concentration of Malate D.,Is the reaction Spontanuous? Choices: No, because RTInQ is very positive Yes, because RTlnQ is very…The KMof the enzyme for the substrate adenosine is 3 × 10ꟷ5M. The product inosine acts as an inhibitor of the reaction, with an inhibition constant (KI, the dissociation constant for enzyme-inhibitor binding) of 3 × 10ꟷ4M. However, a transition state analog,Inhibits the reaction with KIof 1.5 × 10ꟷ13M. Explain why 1,6-dihydroinosine serves as a better inhibitor of adenosine deaminase than inosine. Elaborate on your answe
- The following phenylboronate is a competitive inhibitor of a chymotrypsin-like enzyme. Unlike carbon, boron is quite happy to be bonded to three oxygens (and one carbon)—explain why this feature makes it a much better inhibitor than the corresponding carboxylic acid (which is quite ineffective).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?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.