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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- The Reactions and Meehanisms of the Leloir Pathway Write the reactions that permit galactose to be utilized in glycolysis. Write a suitable mechanism, tor one of these reactions.a What would be the appropriate name for an enzyme that catalyzes each of the following reactions: b H3C iOH OH NH₂ alanine ligase alanine oxidoreductase alanine isomerase alanine transferase OH H3C CH3 H3C NO₂ propanone transferase propan-2-ol hydrolase propan-2-ol oxidoreductase propan-2-ol isomerase OH H3C CH3In step 2 of the fatty acid biosynthesis, the acetyl-S-synthase condenses the acetyl group (C2) with a malonyl-ACP (C3) and subsequent decarboxylation to acetoacetyl-ACP (C4). Give the molecule [A] after condensation and before decarboxylation in the reaction below. synthase (A] ACP + CO2 + HS synthase ACP HO S.
- 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 purinosome contains enzymes that convert the serine hydroxymethyl group to the formyl group of 10-formyltetrahydrofolate. Write a balanced equation for each reaction in this conversion.(i) Describe the mechanism of chymotrypsin in cleaving a peptide bond, highlighting the roles of the catalytice triad for the two phases of the catalytic reactions. Explain the significance of the oxyanion hole for the catalysis. (ii) All serine proteases contain the catalytic triad and these amino acids are positioned in the exact same conformation. Since this is true, why do trypsin and chymotrypsin have such different substrate specificity? What features of the enzyme allow for this situation?
- Consider the following mechanism: What kind of reaction is occurring during this step of glycolysis? What metabolite is in Box 1? What metabolite is in Box 2? What metabolite is in Box 3? What enzyme catalyzes this reaction? Circle and label one place on the mechanism where covalent catalysis is occurring. Suggest an amino acid that could fill the role of residue “A” in the mechanism above and draw its structure at pH 7.4. Suggest an amino acid that could fill the role of residue “B” in the mechanism above and draw its structure at pH 7.4. Under standard conditions, this reaction is unfavorable (DG¢° = 23.8 kJ/mol). What conditions in the cell allow for the actual free energy change to be lower (DG » 0), making the reaction readily reversible? Explain your answer. *please help and explain as well as you can*complete the following mechanism showing the cleavge of the peptide bond for the following cysteine protease reaction. you only need a catalytic dyad for cystein proteases because the pKa of cysteine is low enough (8) and close enough to the pH of 7.4 that is can easily be deprotonated by histidine.Give the product of this reaction sequence: NH3* Bg-CH3 Bg SH (cobalamin) Adenosyl-S H₂C-NH OH A Adenosyl-O intermediate D HN-CH3 Adenosyl-NH HS SH B ATP O-CH3 PPP₁ H3C-S+ Adenosyl H₂N E Adenosyl-O product OH с NH₂ S-CH3
- 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.Predict the locations of 14C in Aspartate synthesis using the following labeled 14C succinate. -OO14C-CH2-14CH2-14COO-Show the structure of each intermediate in the conversion of b-hydroxybutyryl-ACP to butyryl-ACP by the fatty acid synthetase complex. Show where cofactors participate. In your first intermediate, circle the carbon atoms derived from malonyl-CoA.