7) the amino acid below attached to PLP as an imine. Hydrolyze the product amino acid off with water. Don't worry about stereochemistry. Show how PLP can carry out the following conversion. Start the mechanism with PLP, H20 H NH3 CO2H + PI NH2 H OH
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PLP or Pyridoxal phosphate is an enzyme which has the ability to act as an electrophilic catalyst that stabilizes different types of carbanionic reaction intermediates. It catalyzes myriad reactions and forms internal lysine derived aldimine.
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- Draw the Fischer projection for L-glucose. Drag the appropriate labels to their respective targets. H as OH H =0 C CH₂OH Reset Helpcomplete the following mechanism showing the cleavge of the peptide bond for the following cysteine protease reaction. you only need a catalytic dyad for cystein proteases because the pKa of cysteine is low enough (8) and close enough to the pH of 7.4 that is can easily be deprotonated by histidine.When a nonapeptide undergoes partial hydrolysis, it forms dipeptides, a tripeptide and two tetrapeptideswhose amino acid compositions are shown. Reaction of the intact nonapeptide with Edman’s reagentreleases PTH-Leu. What is the sequence of the nonapeptide?1. Pro, Ser 3. Met, Ala, Leu 5. Glu, Ser, Val, Pro 7. Met, Leu2. Gly, Glu 4. Gly, Ala 6. Glu, Pro, Gly 8. His, Val
- In a solution with pH ~7 most of the amino acids are form zwitterions. Name the amino acids which are charged positively and negatively and draw them in ionized forms.Which Ami no acids can be found in the following peptide?The following is the chemical structure of nicotinamide adenine dinucleotides, a coenzyme commonly used in enzymatic reactions. Но 4 HO 0-P-0 *Na "O. `NH2 N 1 "OH H2N OH Which of the indicate regions is the site of the redox activity of this coenzyme? 2.
- NoneCopy of The following reaction scheme shows the states of the amino acid hisitdine. Histidine has three pKa's - 2, 6 and 9.2. Which form of Histidine predominates at pH of 5? *H3N-CH-Ĉ-OH CH2 *H3N-CH-C–O- CH2 "H3N-CH-C-O- CH2 H2N-CH-C–O- CH2 +HN *HN N' -NH -NH -NH NH A C O A. A ОВ. В OC.C O D.D O E. The answer cannot be determined with information given.From the oligopeptide below, write completely the amino acids and/or peptide fragments that resulted from the reaction of elastase. The amino acids and residues should be represented by the three-letter abbreviation.
- The synthesis of compound 6 proceeds via the metabolic pathway given below. Which enzyme is most suitable for controlling the synthesis of compound 6 by feedback inhibition? Which compound is most likely to be a negative modulator of this enzyme? Which compound is most likely to be a positive modulator of this enzyme?a What bond is hydrolyzed in the synthesis of CAMP? the bond between the carbon atom of ribose and the nitrogen atom of adenosine the bond between the a phosphorus atom and the oxygen atom of ribose the phosphate anhydride bond between the 3 and y phosphorus atoms the phosphate anhydride bond between the a and phosphorus atoms Submit b What bond is formed in the synthesis of CAMP? the bond between the B-phosphorus and the 5'- hydroxyl group of ribose the bond between the B-phosphorus and the 3'- hydroxyl group of ribose the bond between the a-phosphorus and the 5'- hydroxyl group of ribose the bond between the a-phosphorus and the 3'- hydroxyl group of riboseguanosine and a water bind in the active site, does not matter in which order. The scissile N-1 glycosidic bond between the anomeric carbon and N9 of the base is broken resulting in an oxocarbenium transition state. The leaving group electrons are not protonated, but instead swing up to form a double bond between N9 and C8. The double bond that is already present on the purine swings out on N7 and is protonated by an active site histidine acting as a general acid. An active site aspartate acts as a general base, and deprotonates the water substrate molecule. The deprotonated water is then free to attack the transition state in a manner that will generate an αribose. Draw the active site and show how the mechanism works. You will need to draw 3 or 4 different active site “snap-shots” to show the entire process. Be sure to clearly show the transition state and how it might be stabilized