On the basis of the information provided in the figure, show the next step in the mechanism for peptide-bond cleavage by a cysteine protease. Cysteine proteases
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- complete 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.Using the catalytic mechanism of serine proteases, draw and label a reaction coordinate diagram/graph of the chymotrypsin-catalyzed hydrolysis of a peptide bond.In 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 respectively
- (i) Describe the mechanism of chymotrypsin in cleaving a peptide bond, highlighting the roles of the catalytice triad for the two phases of the catalytic reactions. Explain the significance of the oxyanion hole for the catalysis. (ii) All serine proteases contain the catalytic triad and these amino acids are positioned in the exact same conformation. Since this is true, why do trypsin and chymotrypsin have such different substrate specificity? What features of the enzyme allow for this situation?If the substrate for an enzyme catalyzed reaction contained a negative charge, which of the following amino acids would most likely be present in the active site to provide electrostatic destabilization of the ES complex? Leu Val O Asp O LYS QUESTION 15 What is the function of the histidine in the diagram of the mechanism at right with the substrate, a phenylalanine residue? (n) His Asp Nucleophilic affack by water stabilization of a metal ion covalent catalysis electrostatic attraction of the substrate O acid base catalysis 789 Mustly cloudy Click Save and Submit to save and submit. Click Save All Ansuwers to save all answers. here to searchIn this step of purine biosynthesis, which functional group gets activated by ATP Pribose NH, ATP Carboxyaminolmidazole ribonedeotide Asp AD Fumarate Pribose NH, S-Aminolmidazole- 4(N-succinylcarboxamide) ribonucleotide O Carboxyaminoimidazole ribonucleotide COOH O Carboxyaminoimidazole ribonucleotide NH2 O Asp side chain COOH O Asp main chain NH2 O Asp main chain COOH
- 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 Adraw the complete mechanism of lysozyme (SN2) beginning with the disaccharide N-acetyl muramic acid - to N acetyl glucosamineThe rate of the peptidyl transferase reaction increases as the pH increasesfrom 6 to 8. Explain these results in terms of its reaction mechanism.
- erioiogy e cell walls of Gram-positive and Gram-negative bacteria are structurally different but both contain peptidoglycan. Which TWO of the following statements about peptidoglycan biosynthesis are CORRECT? O Peptidoglycans are made from alternating units of N-acetylmuramic acid and N-acetylglucosamine. O N-acetylglucosamine is synthesised from N-acetylmuramic acid by the addition of acetic acid derived from phosphoenolpyruvate. O Peptidoglycan synthesis in Gram-positive bacteria involves the addition of the amino acids, L-alanine, D-glutamic acid, L-lysine, to N-acetylmuramic acid. O D-glutamic acid-D-glutamic acid dipeptide is linked to the tripeptide side chain of N-acetylmuramic acid to form N-acetylmuramic acid-pentapeptide O At the beginning of the biosynthesis pathway, the N-acetylglucosamine-N-acetylmuramic acid-pentapeptide-phospholipid crosses the cell membrane and is added to growing peptidoglycan chain. O The transglycosylase enzyme is located on the inner face of the…The glycosaminoglycan polysaccharide chainsthat are linked to specific core proteins to form the pro-teoglycan components of the extracellular space arehighly negatively charged. How do you suppose thesenegatively charged polysaccharide chains help to estab-lish a hydrated gel-like environment around the cell? Howwould the properties of these molecules differ if the poly-saccharide chains were uncharged?Proteases are enzymes that cleave peptide bonds using general acid–base catalysis. General acid–base catalysis relies on a proton donor or acceptor other than water. Proteases rely on proton transfer to create strong nucleophiles from active-site amino acid residues. In the protease chymotrypsin, an active-site serine is a potent nucleophile. A nearby residue, His 57, interacts with serine to increase its reactivity. A schematic of chymotrypsin’s active site illustrates the active site Ser 195 and His 57 R groups. The Asp 102 residue helps position the His 57 residue via hydrogen bonding.