Put the steps of the chymotrypsin's enzymatic reaction in order of events from #1-10. -Tetrahedral intermediate collapses and product 2 released. -Aromatic R group of polypeptide substrate is positioned in hydrophobic pocket and the carbonyl of that residue is positioned in the oxyanion hole -His57 deprotonates Ser195 -Formation of acyl-enzyme intermediate -Triad in original form with Asp102 hydrogen bonding with His57 and His57 hydrogen bonding with Ser 195. -Tetrahedra intermediate collapses and product 1 released -H2O enters active site of chumotrunsir -Ser195 does nucleophilic attack on carbonyl of substrate positioned in oxyanion hole -His57 deprotonates H20 -H20 does nucleophilic attack on carbonyl of substrate in oxyanion hole

Put the steps of the chymotrypsin's enzymatic reaction in order of events from #1-10. -Tetrahedral intermediate collapses and product 2 released. -Aromatic R group of polypeptide substrate is positioned in hydrophobic pocket and the carbonyl of that residue is positioned in the oxyanion hole -His57 deprotonates Ser195 -Formation of acyl-enzyme intermediate -Triad in original form with Asp102 hydrogen bonding with His57 and His57 hydrogen bonding with Ser 195. -Tetrahedra intermediate collapses and product 1 released -H2O enters active site of chumotrunsir -Ser195 does nucleophilic attack on carbonyl of substrate positioned in oxyanion hole -His57 deprotonates H20 -H20 does nucleophilic attack on carbonyl of substrate in oxyanion hole

Biochemistry

6th Edition

ISBN:9781305577206

Author:Reginald H. Garrett, Charles M. Grisham

Publisher:Reginald H. Garrett, Charles M. Grisham

Chapter27: Metabolic Integration And Organ Specialization

Section: Chapter Questions

Problem 20P: Figure 27.3 illustrates the response of R (ATP-regenerating) and U (ATP-utilizing) enzymes to energy...

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The oxyanion hole deprotonates an incoming water molecule to convert it to a potent nucleophile. True or False? The oxyanion hole is comprised of hydrogen bonding atoms that project into a space on the active site that will have all H-bonding potential satisfied only during the catalytic cycle of the reaction. True or False? The catalytic triad residues are all next to each other in the primary sequence of trypsin. True or False?
Trypsin contains a/an [aspartate/serine/histidine] in its specificity pocket to attract lysine and arginine side chains. It contains a potent nucleophilic [histidine/serine/aspartate] in its active site that is capable of attacking the electrophilic [carbon/nitrogen/oxygen] of the closest peptide bond. The [acyl-enzyme/specificity pocket/oxyanion] transition state is stabilized by the backbone amide hydrogens of glycine and serine. In this way, the enzyme is able to catalyze the [hydrolysis/ligation/metalysis/hydrogenation] of the peptide bond.
______ 1. is a serine protease that cuts the peptide after aromatic amino acids______ 2. is a type of chemical bond formed by chymotrypsin with its substrate as a first step in the reaction mechanism______ 3. is the name of the compound that hydrolyzes the chemical bond formed between chymotrypsin and its substrate ______ 1. is the name of the inactive form of chymotrypsin
During chymotrypsin-mediated catalysis, which of the following statements is true? Select any/all answers that apply. A. A basic (positively-charged) side chain of the substrate polypeptide sits within the oxyanion hole of the enzyme. B. A basic (positively-charged) side chain of the substrate polypeptide sits within the specificity pocket of the enzyme. C. Ser195 hydrogen-bonds with the backbone carbonyl group of the substrate polypeptide within the oxyanion hole of the enzyme. D. All three residues that comprise the catalytic triad of the enzyme interact directly with the substrate polypeptide chain. E. Both covalent catalysis and acid-base catalysis occur.
In an enzyme's active site, a catalytic histidine residue abstracts a proton from the hydroxyl group of a catalytic serine residue. The catalytic serine then performs a nucleophilic attack on the carbonyl carbon of a peptide bond (on the substrate). The final products of this reaction are a cleaved substrate at the peptide bond, with a new amino group and carboxyl group, and regenerated catalytic residues. In this reaction, the serine residue is displaying what? A. Proximity and Orientation B. Covalent catalysis C. Metal ion catalysis D .A and B E. B and C F. None stated here
help fill in the word between brackets Serine proteases are an example of [nucleophilic/electrophilic/covalent/acid- base] catalysts because the catalytic triad [aspartate/serine/histidine] protonates the leaving group and abstracts a proton from water. Serine proteases are an example of [nucleophilic/electrophilic/covalent/acid-base] catalysts because the catalytic [aspartate/serine/histidine] is converted to an oxyanion to attack the peptide bond. Serine proteases are an example of [nucleophilic/electrophilic/covalent/acid-base] catalysts because an acyl-enzyme intermediate is formed during the catalytic cycle between part of the substrate and the catalytic [aspartate/serine/histidine].
In the first step of the aldolase reaction, an active site Lys229 residue, with its side chain amino group in the deprotonated state, acts as a nucleophile and attacks the carbonyl C2 carbon of fructose 1,6-bisphosphate to form a Schiff base (boxed in the scheme). Since the pKa of the Lys side chain amino group in free solution is ~10.5, the pKa of Lys229 side chain must have been perturbed to a (higher lower) value for the enzyme to be active at neutral pH. the answer should include sufficient details, including the definition of pKa.
A histidine was determined to be the critical residue involved in an enzyme-catalyzed reaction. If the pKa of the histidine is known to be 6.5 in the active site and the pH of maximum catalytic activity is 7.2, what is likely the primary role of histidine in the catalytic reaction? A. forms a covalent bond with the substrate B. reduces the entropy of the substrate C. stabilizes a charged intermediate D. acts as a proton donor Aspartate and lysine are in the active site of an enzyme. They are both known to participate directly in catalysis. The pKa's of the residues are found to be 3.2 and 9.6, respectively for aspartate and lysine. The optimum pH for the enzyme is 6.4. Which forms of these two residues will predominate when the enzyme is most active? A. aspartate is protonated; lysine is deprotonated B. both residues are deprotonated C. aspartate is deprotonated; lysine is protonated D. both residues are protonated
Draw the catalytic triad of a serine protease at the first tetrahedryl intermediate stage. Your drawing should include the amino acids that make up the triad, any part of the substrate that should be present, and any other molecules that are present in the active site.
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
Enzyme X exhibits maximum activity at pH = 6.3. X shows a fairly sharp decrease in its activity when the pH goes much lower than 5.8. One likely interpretation of this pH activity is that: a Glu residue on the enzyme is involved in the reaction. a Tyr residue on the enzyme is involved in the reaction. a His residue on the enzyme is involved in the reaction the enzyme uses NADH has a cofactor. the enzyme uses coenzyme A has a cofactor.
for the following reactions: arrive at the Michaelis menten enzyme kinetics: E+2A <-----k1,k2----->A.E+A reversible A.E+A<------k3,k4------>A 2E reversible A2.E------k5--------> E+CD non-reverisble show all steps