The thiamine pyrophosphate (TPP)-dependent enzyme benzoylformate decarboxylase catalyzes the decarboxylation of benzoylformate to yield benzaldehyde. Propose a mechanism based on your knowledge of TPP-dependent mechanisms. You may begin the reaction with the ylid form of TPP and you only need to show the structure of the “business end” of TPP. Show all electron flow using the arrow convention.

The thiamine pyrophosphate (TPP)-dependent enzyme benzoylformate decarboxylase catalyzes the decarboxylation of benzoylformate to yield benzaldehyde. Propose a mechanism based on your knowledge of TPP-dependent mechanisms. You may begin the reaction with the ylid form of TPP and you only need to show the structure of the “business end” of TPP. Show all electron flow using the arrow convention.

Organic Chemistry

9th Edition

ISBN:9781305080485

Author:John E. McMurry

Publisher:John E. McMurry

Chapter29: The Organic Chemistry Of Metabolic Pathways

Section29.SE: Something Extra

Problem 30MP

See similar textbooks

Similar questions

Triosephosphate isomerase (TIM) catalyzes the conversion of dihydroxyacetone phosphate to glyceraldehyde-3-phosphate. The enzyme’s catalytic groups are Glu 165 and His 95. In the first step of the reaction, these catalytic groups function as a general-base and a general-acid catalyst, respectively. Propose a mechanism for the reaction.
The overall adenylate kinase reaction (2 ADP = AMP + ATP) is a combination of 3 reactions: ATP hydrolysis, pyrophosphate hydrolysis, and ATP formation. Show each step and provide the standard free energy (ΔG°′) for each and the overall reaction. If the adenylate kinase reaction is at equilibrium and intracellular [ATP] = 5 mM and [ADP] = 0.5 mM, calculate the concentration of AMP at pH 7 and 25 °C. Show all work. ATP (ADP+P) = -30.5 kj/mol; ATP (AMP+PP) = -45.6 kj/mol; PP = -19.2 kj/mol
The following compound has been found to be an inhibitor of penicillinase. The enzyme can be reactivated by hydroxylamine (NH2OH). Propose a mechanism to account for the inhibition and for the reactivation.
Suggest a mechanism of enzyme catalysed reaction.
The stability of our genetic code depends on the stability of DNA. We are fortunate that the aminoacetal linkages ofDNA are not easily cleaved. Show why your mechanism for part (a) does not work so well with deoxycytidine anddeoxyadenosine.
This reaction is also an important reaction of the tricarboxylic acid cycle in cells, wherein the reaction occurs in neutral solution, so the acid groups are both ionized to the carboxylate form. The reaction is catalyzed by the stereospecific enzyme fumarase that utilizes only the trans form of 2-butenedioate ion (also known as fumarate) and produces only the (S)-2-hydroxysuccinate enantiomer (also known as (S)-malate). Draw the correct stereochemical structures of these two compounds of the fumarase-catalyzed reaction. Be sure to include all hydrogen atoms and show the carboxylates as anions.
The phosphoryl group on phosphoglucomutase is slowly lost by hydrolysis. Propose a mechanism that utilizes a known catalytic intermediate for restoring this essential phosphoryl group. How might this phosphoryl donor be formed?
please explain why this happends, im having trouble in this section. Part A Chymotrypsin, an enzyme that hydrolyzes peptide bonds in proteins, functions in the small intestine at an optimum pH of 7.7 to 8.0. How is the rate of the chymotrypsin-catalyzed reaction affected by each of the following conditions?
Polyunsaturated fatty acids (PUFA's) in oils 0.g. sunflower oil are prone to rancidity because they contain conjugated double bond systems which are easily oxidized in the presence of light or peroxides. BHT Is used as an antioxidant in oils to prevent oxidative rancidity. How do BHT prevent oils from reacting with peroxides so that they do not become rancid? Show the mechanism.
The rate constant for the uncatalyzed reaction of two molecules of glycine ethyl ester to form glycylglycine ethyl ester is 0.6 M- 1s - 1. In the presence of Co2 +, the rate constant is 1.5 * 106 M- 1s - 1. What rate enhancement does the catalyst provide?
When some sugars dissolve in water they spontaneously undergo changes in optical rotation called mutarrotation. The Mutarrotation of D-glucopyranose is catalyzed by acid and bases. 2-Hydroxypyridine is a more effective catalyst than phenol and pyridine for this reaction because: a.Both oxygen and N in 2-hydroxypyridine act as bases increasing the rapid interconversion of sugar b. The OH of 2-hydroxypyridine serves as the base while the current N as the acid. c. 2-hydroxypyridine acts both as a base to remove the proton from the hydroxyl group in the hemiacetal and as an acid to provide a proton to the oxygen in the hemiacetal. d.Phenol and pyridine are very expensive.
One of the steps in the biosynthesis of uridine monophosphate is the reaction of aspartate with carbamoyl phosphate to give carbamoyl aspartate followed by cyclization to form dihydroorotate. Propose mechanisms for both steps.