Summarize what is happening in step 3 of deoyribonucleotide synthesis via RNR (below). Include the catalytic mechanisms used to enhance the rate of the reaction. OH OH OH HO- H₂O SH SH HO- SH -00
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- Please determine the template sequence used in a pyrosequencing reaction in the following graph. A 4G T 2G C 3T 4G 2T G CA G 2T G 3 2 min AGT CA G T C A G T C A G T C A GT C AG T c A G 0.5 pmolWhich of the following would be a good chemotherapy approach: blocking formationof the ribonucleotide GTP or blocking formation of the deoxyribonucleotide dGTP?Why? Please explain the chemical differences between each of the two nucleotides. Use the specific processes below to support your choice by explaining how either GTP or dGTPare related to these and how loss of the particular molecule would affect each process. *PEP carboxykinase in gluconeogenesis*Succinyl-CoA synthetase in the TCA Cycle*Glucagon signal transductionCan you please order the following steps involving the regeneration of ribonucleotide reductase that occurs in most animals so that it may carry out the formation of deoxyribonucleotides. (Note that not all steps are shown.) 1. Reduction of thioredoxin 2. Reduction of ribonucleotide reductase 3. Oxidation of thioredoxin reductase 4. Reduction of thioredoxin reductase
- Chart is Given for you: Below is a chart of values for actual enzymes. Enzyme Km (M) kcat (1/s)Chymotrypsin 1.5 × 10^−2 0.14Pepsin 3.0 × 10^−4 0.5Tyrosyl-tRNA synthetase 9.0 × 10^−4 7.6Ribonuclease 7.9 × 10^−3 7.9 × 10^2Carbonic anhydrase 2.6 × 10^−2 4.0 × 10^5Fumarase 5.0 × 10^−6 8.0 × 10^2 Assume the enzyme concentration is equal across all samples (and is equal to 1). (Answer a and b only)a. Which enzyme will have the highest V0 at very high substrate concentrations? (1 M). Why? b. Which will have the highest V0 at very low substrate concentrations (5.0 × 10^−12). Why?The following is a simple biochemical pathway. enzyme AB enzyme CD X → Y Z A nonsense mutation occurs in the AB sequence. What would be the most significant outcome of this?E. coli ribonuclease H1 is an enzyme that catalyzes the hydrolysis of phosphodiester bonds in RNA. Its proposed mechanism involves a 'carboxylate relay,' as shown below. His124 Asp70 || -HN-CH-C -HN-CH-C- CH2 CH2 c=0 RNA substrate HN H. H. (1) Fill the blanks. In the reaction scheme above, His124 acts as a ( ). The purpose of this relay system is to deprotonate the water molecule (II) so that it becomes a better ( :0
- The text states that in E. coli ribonucleotide reductase Tyrosine-122 was identified as the source of the catalytically essential free radical. Describe experimental evidence that would support this conclusion.Present a scheme for the deoxyribonucleotide biosynthesis and explain the mechanism of the ribonucleotides transformation into deoxyribonucleotides .Which 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.
- (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 objective is to study a novel protease P isolated from the digestive tract of an Amazonian insect. This protease can exist into two forms Pi and Pa which have identical amino acid sequences (both of 80 kDa). However, only Pa shows proteolytic activity. To better understand the activation mode of Pi (inactive form) in Pa (active form), the following experiment was done using DIPF. DIPF (diisopropylphosphofluoridate) is a well-known irreversible inhibitor of serine proteases. It reacts with the catalytic serine residue of the active site of proteases as shown below: Enzyme -CH₂OH + CH(CH3)2 O F-P=0 O CH(CH3)2 Diisopropylphospho- fluoridate (DIPF) Enzyme -CH,—O CH(CH3)2 O <=0 O CH(CH3)2 DIP-Enzyme Both proteases Pa and P₁ were incubated with 32P-DIPF for 30 min at 37°C, and then dialysed to remove excess of unreacted radiolabelled reagent. The two proteases were then analyzed in Sodium Dodecyl Sulphate-Polyacrylamide Gel Electrophoresis (SDS-PAGE), with and without 2-mercaptoethanol.…Your are working in a biodiesel production plant and are trying to optimize the production of biodiesel (Fatty Acid Methyl Esters). The enzyme lipase catalyzes a key step in this reaction (See below). You are tasked with mutating a recombinant lipase to improve the efficiency of the reaction to improve yields of the Fatty Acid Methyl Esters. Which kinetic parameters would you calculate to determine the efficiency of the mutate enzymes. Briefly explain the design of an experiment to calculate these parameters. LIPASE + H,C-OH Lipase production Vegetable oil Methanol Biodiesel Transesterification -OH R HO. Lipase + R2 HO. HO, Triglyceride Fatty acids Glycerol