1. Shown below is the intermediate in the aldolase mechanism, after dissociation of the firstproduct (GA-3P). Draw resonance structure of this intermediate showing the carbanion speciesAND the arrow movement that associated with formation of this resonance structure.CH₂OPO²-H 1Lys-N-C||-B-H:A-H-BCovalent enzyme-enamine intermediate

When drawing chemical reaction mechanisms, we use a curved arrow to show the flow of electrons. The…

Answered: 1. Shown below is the intermediate in…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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Gluconeogenesis uses just the carbon skeleton of amino acids, not fatty acids. So, how does fatty acid oxidation in the liver produce brain fuel? Describe the processes and chemicals that are involved.
During the inhibition of glycopeptide transpeptidase, a serine from the enzyme reacts with the amide carbonyl of the lactam ring in penicillin antibiotic to form an enzyme - penicillin complex which inactivates the enzyme. The conversion of an amide to an an ester is not normally observed in reactions of carboxylic acid derivatives. Provide an explanation as to why the amide of a penicillin antibiotic can react with the serine of glyopeptide transpeptidase in this unexpected way.
Which strategies listed does this enzyme use to facilitate cleavage of α-galactoside? Choice 1 of 6:Dehydration synthesis Choice 2 of 6:acid base catalysis Choice 3 of 6:covalent catalysis Choice 4 of 6:metal ion catalysis Choice 5 of 6:stabilizing the transition state Choice 6 of 6:binding with high affinity to the product
In many biochemical reactions which involves the formation of an enolate intermediate, the carbonyl oxygen of the substrate is coordinated to a divalent metal ion (usually zinc or magnesium) in the active site. Explain with structural drawings, how this ion-dipole interactions affect the acidity of the a-protons?
The enzyme which catalyzes the reaction below belongs to which enzyme classification? Н.С— ОН HC=0 C=0 Н-С—ОН H,C-0-P-o- || H,C –0-P-0- O Transfera Hydrolase Isomerase Oxidoreductase
In the pyrimidine degradative pathway, all pyrimidines undergo conversion to uracil, which undergoes an NADPH-dependent reduction. Show plausible reactions leading from cytidine, cytosine, and uridine to uracil, and write a plausible structure for the product of uracil reduction (dihydrouracil).
Identify the substrate, enzyme, and products in the following chemical reaction: HO но. HO но, HO HO OH HO Lactase NO2 он NO2 OH ONPG p-D-Galactose O-Nitrophenol o-Nitrophenol (ONP) 1. Products B-D-Galactose 2. Substrate Lactase 3. Enzyme ONPG
C Phosphoglycerate enolase coo O H-C-O-P=O CH₂OH 2-Phosphoglycerate This is a (an) d Tyrosine hydroxylase HO coo NH3 L-Tyrosine This is a (an) 0₂ coo C-O-P-C || CH₂ Phosphoenolpyruvate H₂O + HO HO L-DOPA H₂O coo NH3
7. Chalcone isomerase catalyzes the reaction illustrated below. A series of modification experiments were performed on this enzyme to identify which amino acid residues might be in the active site and which might promote the cyclization reaction. OH Ho. Но Explain the following results: A) Acetic anhydride treatment inhibited enzyme activity. B) Pyrocarbonate inhibited activity and was found to modify 7 residues. However, this enzyme only contains 6 His and modification of these did not affect activity. C) lodoacetate inhibited activity but this effect coult be decreased in the presence of substrate or product. D) Methane methanethiol sulfonate modified the enzyme but did not inhibit catalytic turnover. In addition, this modification was reversed in the presence of B-mercaptoethanol. keNyons Rengent
3. The enzyme enolase catalyzes the removal of one water molecule ("dehydration") of 2- Phosphoglycerate (2-PGA). The numbering scheme of the enolase carbons is labeled HC-0-P-O + H20 on 2-PGA. || CH2 HO-CH2 2-Phosphoglycerate Phosphoenolpyruvate Part of the catalytic mechanism is as follows: Mg2+ PO?- Mg?+ PO? 'o. Ó H Mg?+ Mg²+; PO? :-C-H C=C-C-H OH OH Нон Enolase но но H-N*-H Lys345 Lys345 Glu211 Glu211 2-Phosphoglycerate bound to enzyme Enolate intermediate Phosphoenolpyruvate а. Draw the mechanism of the reaction by adding arrows to show how electrons move. Mg2+ PO?- Mg2+ po PO H H Mg2+ С -с-с-н Mg2+ C=c-C-H H OH OH Enolase H. H-N-H но но .. H-N-H Lys345 Lys345 Glu211 Glu211 2-Phosphoglycerate bound to enzyme Enolate intermediate Mg?+ PO O. он Mg2+: PO? c=C-C-H OH HOH H но C=C H-N*-H Lys345 Glu211 Enolate intermediate Phosphoenolpyruvate
1. Acid phosphatases are an important group of enzymes that can be detected in human bloodserum. Under slightly acidic conditions (pH 5.0), this group of enzymes can hydrolyzebiological phosphate esters as follows:R-O-P-O3-2 + H 2O R-OH + HO-P-O3-2.Acid phosphatases are produced and can be detected in erythrocytes, kidney, spleen, the liver,and prostrate gland. The enzyme from the prostrate gland is clinically important because anincreased activity in the blood is frequently an indication of cancer of the prostrate gland.Tartrate ion can strongly inhibit the phosphatase from the prostrate gland, but not acidphosphatases from other tissues. How can you use the information above to develop a specificprocedure for measuring the activity of the acid phosphatase of the prostrate gland in humanblood serum?
Carboxylic acids, such as the one shown below, can be difficult to reduce Provide the name of a reductant A. Explain why this reductant is able to react with the carboxylic acid whereas others cannot (Hint: Draw and discuss the potential reactive intermediates/transition states).

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