If the substrate for an enzyme catalyzed reaction contained a negative charge, which of the following amino acidswould most likely be present in the active site to provide electrostatic destabilization of the ES complex?LeuValO AspO LYSQUESTION 15What is the function of the histidine in the diagram of the mechanism at right with the substrate, a phenylalanineresidue?(n)HisAspNucleophilicaffack by waterstabilization of a metal ioncovalent catalysiselectrostatic attraction of the substrateO acid base catalysis789 Mustly cloudyClick Save and Submit to save and submit. Click Save All Ansuwers to save all answers.here to search

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Biochemistry

6th Edition

ISBN:9781305577206

Author:Reginald H. Garrett, Charles M. Grisham

Publisher:Reginald H. Garrett, Charles M. Grisham

Chapter17: Metabolism: An Overview

Section: Chapter Questions

Problem 6P: Why Do Anabolic and Catabolic Pathways Differ? Why is the pathway for the biosynthesis of a...

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Why Do Anabolic and Catabolic Pathways Differ? Why is the pathway for the biosynthesis of a biomolecule at least partially different from the pathway for its catabolism? Why is the pathway for the biosynthesis of a biomolecule inherently more complex than the pathway for its degradation?
The active site of an enzyme that uses a general acid-base catalytic mechanism contains a Glu and an Asp residue (both of which are essential for catalysis) with pKa values of 5.9 and 4.5, respectively. If the enzyme is found in the lysosome (pH = 5.2), which residue will act as the general acid and which will act as the general base during the initial steps of the reaction?
#1 Specify the role each of the following amino acids play within the crystal structure and/or active site for Be as specific as possible, with pictures (and mechanistic arrows) as necessary. His11 Arg140 Glu89 Trp68 #2 Provide a step-wise mechanism for the reaction Bisphosphoglycerate mutase catalyzes, using the amino acids responsible for aiding in catalysis. You do not need to add surrounding amino acids that aid in substrate specificity. (drawn out)
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.
An enzyme contains an active site aspartic acid with a pKa = 5.0, whichacts as a general acid catalyst. On the accompanying template, draw thecurve of enzyme activity (reaction rate) versus pH for the enzyme (assumethat the protein is stably folded between pH 2–12 and that the active siteAsp is the only ionizable residue involved in catalysis). Briefly explain theshape of your curve.
A prokaryotic species is facing a new environmental stressthat can be ameliorated by a catalytic activity that requiresthe side chain of a unique amino acid derivative called pyrovaline. How would such an organism develop a mechanism for the incorporation of this nonstandard amino acidinto an enzyme molecule? What would be the properties ofthe molecules required to solve this problem?
How would chymotrypsin's catalytic triad be affected by extremely low and extremely high pH values (assuming the rest of the protein remains intact)?
Trypsin, a peptidase that hydrolyzes polypeptides, functions in the small intestine at an optimum pH of 7.7–8.0. How is the rate of a trypsin-catalyzed reaction affected by each of the following conditions?
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.
Studies at diff erent pH’s show that an enzyme has two catalytically important residues whose pKs are ∼4 and ∼10. Chemical modifi cation experiments indicate that a Glu and a Lys residue are essential for activity. Match the residues to their pKs and explain whether they are likely to act as acid or base catalysts.
At what substrate concentration would an enzyme with a kcat of 25.0 s-1 and a KM of 3.5 mM operate at 25% of its maximal rate? How many reactions would the enzyme catalyze in 45 seconds when it is fully saturated with substate, assuming the enzyme has one active site?
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

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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 O val O ASP O LyS