The mechanism of chymotrypsin can be viewed as a two-step process, acylation of the enzyme active site followed by adeacylation reaction.What accounts for the observed "burst" in rapid kinetic studies of the hydrolysis of N-acetyl-L-phenylalanine p-nitrophenylester by chymotrypsin?The rate of hydrolysis of the acyl-enzyme intermediate is faster than the rate of forming the acyl-enzyme intermediate.The rates of the acylation and deacylation reactions are equal.The rate of the acylation reaction is slower than the rate of the deacylation reaction.The rate of the acylation reaction is faster than the rate of the deacylation reaction.

A burst in rapid kinetic studies (i.e. pre-steady state studies) is a high rate of product release…

Answered: The mechanism of chymotrypsin can be…

Biochemistry

6th Edition

ISBN:9781305577206

Author:Reginald H. Garrett, Charles M. Grisham

Publisher:Reginald H. Garrett, Charles M. Grisham

Chapter23: Fatty Acid Catabolism

Section: Chapter Questions

Problem 21P: Using the ActiveModel for enoyl-CoA dehydratase, give an example of a case in which conserved...

See similar textbooks

Similar questions

Using the ActiveModel for enoyl-CoA dehydratase, give an example of a case in which conserved residues in slightly different positions can change the catalytic rate of reaction.
Draw a schematic illustration of the hydrolysis of N-acetylphenylalaninamide catalyzed byalpha-chymotrypsin in which you indicate the important catalytic residues in the active site and how thesubstrate undergoes transformation to products through two different tetrahedral intermediates.
Enolase catalyzes the reversible reaction shown below. Draw the detailed mechanism for the reaction that occurs in gluconeogenesis, namely the reaction of phosphoenolpyruvate to form 2-phosphoglycerate (the reverse direction in the reaction below).
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.
UDP-glucuronosyltransferase enzymes bind the organic compound UDP-glucuronic acid (UDP-GA) in order to catalyse the transfer of a glucuronic acid group from UDP-GA to a drug molecule, releasing UDP from the active site as a product. UDP is then regenerated by the activity of another enzyme. What terms could be used to describe UDP-GA?
In some organisms, isoleucine can be synthesized in a multi-step procedure (a series of enzymatic reactions), beginning with a molecule of threonine. Keeping that in mind explain the experimental results below. Amount of endproduct Activity of threonine (isoleucine) deaminase None Low Medium High Very high High Moderate Very low
Why might the compound shown below acts as a transition state analog of phosphoenolpyruvate carboxykinase. Explain. A drawing of a normal transition state for this enzyme is needed.
Draw the products of the reaction of xylulose-5-phosphate and erythrose-4-phosphate catalyzed by transketolase in the pentose phosphate pathway. Provide the structure in the protonation state found in physiological conditions. H H H OH FO HO-H H-OH H OPO3²- Q transketolase Draw glyceraldehyde-3- phosphate H H- H H H O OH OH OPO3²- Draw fructose-6- phosphate Q I I
Order the cofactors based on their use in the mechanism of the a-etogluterate dehydrogenase complex. 1. Stabilizes a carbanion due to decarboxylation 2. Allows for the splitting of the carbon skeleton from the electron pair generated in a redox reaction 3. Enzyme bond electron carrier that is part of dihydrolipoyl dehydrogenase 4. Final electron acceptor in the overall reaction catalyzed by this complex 1 2 3 4 answer choices: lipoamide, biotin, 2 Fe - 2S cluster, TPP, NAD+, FAD
Glucosidase I catalyzes hydrolysis of specific glucosidase I is a synthetic trisaccharide, glucose-al-2- glucose-al-3-glucose-a-O(CH₂) #COOCH3. Kinetic measurements oligosaccharides containing glucose. obtained using this trisaccharide as substrate in the deoxynorjirimycin at concentrations of 50 μM (), 100 μM absence (x-x) and presence of the inhibitor 1- A) were used to prepare the (-), and 200 μM (4 Lineweaver-Burk plot below: b) Page 3 12) 7. a) V/V (nmol/hr)-1 1.S 1.0- 0.5 1/Trisaccharide (mM)-! Estimate the values for Vmax and KM for the trisaccharide substrate in the absence of the inhibitor. 0.0 -1.0 0.0 One substrate for 1.0 2.0 Determine whether inhibition by 1-deoxynorjirimycin is competitive, non-competitive or neither.
The enzyme Glucose-6-phosphate dehydrogenase catalyzes the nicotinamide adenine dinucleotide oxidation of cyclic glucose-6-phosphate to form the lactone product shown below. Propose a mechanism for this reaction showing all electron flow (using the arrow convention). You must draw the substrate glucose-6-phosphate (the configuration of the anomeric carbon does not matter) and the “business end” of the cofactor.
The reaction catalyzed by phosphorylase is readily reversible in vitro. At pH 6.8, the equilibrium ratio of orthophosphate to glucose 1-phosphate is 3.6. The value of ΔG°’ for this reaction is small because a glycosidic bond is replaced by a phosphoryl ester bond that has a nearly equal transfer potential. However, phosphorolysis proceeds far in the direction of glycogen breakdown in vivo. Suggest one means by which the reaction can be made irreversible in vivo.

SEE MORE QUESTIONS

Recommended textbooks for you

Biochemistry

ISBN:

9781305577206

Author:

Reginald H. Garrett, Charles M. Grisham

Publisher:

Cengage Learning

Biochemistry

ISBN:

9781305577206

Author:

Reginald H. Garrett, Charles M. Grisham

Publisher:

Cengage Learning

SEE MORE TEXTBOOKS