Sulfur compounds give onions their unique flavor and properties. Compound 1 is the starting material for the majority of these flavor components and is converted to Compound 2 under the action of the enzyme alliinase (Reaction 1, unbalanced). +NH3 Compound 1. alliinase Reaction 1 ОН Compound 2
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- Match each of the enzymes involved in de novo pyrimidine synthesis with the correct description: _______ Dihydroorotate dehydrogenase _______ UMP synthase_______ Carbamoyl phosphate synthetase II _______ TMP synthase _______ CTP synthetase_______ Aspartate transcarbamoylase _______ PRPP synthetase (A) attaches an aspartate to an activated carbamoyl molecule(B) bifunctional enzyme that combines a nitrogenase pyrimidine ring to an activated ribose(C) catalyzes the formation of the activated ribose sugar(D) uses glutamine to add an amine to a preformed nucleotide(E) produces the first cyclic nitrogenase ring during de novo pyrimidine synthesis(F) combines bicarbonate and nitrogen from glutamine in the first step of pyrimidine ring synthesis (G) uses a folate derivative to add a methyl group to a preformed nucleotideThe highest energy point of the serine protease reaction is the formation of the tetrahedral oxyanion intermediate on the original carbonyl carbon of the scissile peptide bond. True or False? DIPF is an irreversible inhibitor of serine proteases. True or False? The acyl-enzyme intermediate is the transition state of the reaction. True or False? Serine proteases are classified as isomerases. True or False?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?
- An oligosaccharide is a repeating unit of a-D-galactopyranosyl-(a-1 >3)-allopyranoside. Each disaccharide unit is linked via B-1 --->4 glycosidic bond. The oligosaccharide has 10 monosaccharide residues. Required: Is this oligosaccharide a good substrate for glycolysis? Why or why not? Provide two reasons and discuss corn prehensively.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.Which of the following is a true statement regarding sphingolipid synthesis? (A) The first step in sphingolipid synthesis is the condensation of palmitoyl CoA with aspartate to form b-ketosphinganine.(B) This process requires the reduction of a ketone that uses NADH as the reducing agent.(C) A fatty acid is attached to dihydrosphingosine to form dihydroceramide. (D) FAD is using as an oxidizing agent to remove a double bond from dihydroceramide.(E) The formation of sphingomyelin requires the attachment of a glucose or galactose molecule to ceramide.
- Phosphoglycerate mutase transfers a phosphoryl group from C3 of 3-phosphoglycerate to C2 position to give 2-phosphoglycerate. Why is it important to have the phosphoryl group at position 2 rather than at C3? It was observed that the activity of some preparations of the enzyme could be increased if catalytic (very small) amount of 2, 3-bisphosphoglycerate was added to the enzyme. Give a possible explanation for this observation.The glycine cleavage system is a group of four enzymes that together catalyze the following reaction: Use the following information to determine the sequence of reactions carried out by the glycine cleavage system:a. The first enzyme is a PLP-requiring decarboxylase.b. The second enzyme is aminomethyltransferase. This enzyme has a lipoate coenzyme.c. The third enzyme synthesizes N5,N10-methylene-THF and also forms +NH4.d. The fourth enzyme is an FAD-requiring enzyme.e. The cleavage system also requires NAD+ .Peroxisomes have an alternative pathway for oxidizing polyunsaturated fatty acids. They contain a hydratase that converts D-3-hydroxyacyl CoA into trans Δ²- enoyl CoA. How can this enzyme be used to oxidize CoAs containing a cis double bond at an evennumbered carbon atom (e.g., the cis-Δ¹² double bond of linoleate)?
- Seduheptulose is an intermediate in respiratory and photosynthetic pathways and plays a vital role in the non-oxidative branch of the pentose phosphate pathway. The structure of the Seduheptulose is shown below. Illustrate the two (2) pyranose Haworth projection of the said compound.Which of the following statements is not true about the catalytic triad in chymotrypsin? Group of answer choices the side chain of the serine 195 is hydrogen bonded to the imidazole ring of histidine the -NH group of the imidazole ring of histidine is hydrogen bonded to the carboxylate group of aspartate 102 the histidine residue serves to position the aspartate 102 side chain and to polarize its carboxylate group so that it is poised for deprotonation histidine acts as a general base catalyst none of theseAn inhibitor that specifically labels chymotrypsin at histidine 57 is Ntosylamido-l-phenylethyl chloromethyl ketone. How would you modify the structure of this inhibitor to label the active site of trypsin?