A flavin-dependent enzyme catalyzes the transformation shown below. NH₂ FAD NH₂ a) Circle the specific class of enzymes below to which this flavin-dependent enzyme most likely belongs. oxidase monooxygenase (FMO) b) Circle the co-substrate this enzyme requires for activity. NAD(P)+ NAD(P)H c) Circle the co-product this enzyme produces. H₂O H₂O2 Baeyer-Villiger monooxygenase (BVMO) reductase no co-substrate required Neither d) Provide a complete curved-arrow mechanism for the transformation shown above. You should draw all reaction intermediates in their most stable resonance form wherever possible. Be sure your mechanism shows the formation of all co-products. You may continue your mechanism onto the next page if necessary.

A flavin-dependent enzyme catalyzes the transformation shown below. NH₂ FAD NH₂ a) Circle the specific class of enzymes below to which this flavin-dependent enzyme most likely belongs. oxidase monooxygenase (FMO) b) Circle the co-substrate this enzyme requires for activity. NAD(P)+ NAD(P)H c) Circle the co-product this enzyme produces. H₂O H₂O2 Baeyer-Villiger monooxygenase (BVMO) reductase no co-substrate required Neither d) Provide a complete curved-arrow mechanism for the transformation shown above. You should draw all reaction intermediates in their most stable resonance form wherever possible. Be sure your mechanism shows the formation of all co-products. You may continue your mechanism onto the next page if necessary.

Biochemistry

6th Edition

ISBN:9781305577206

Author:Reginald H. Garrett, Charles M. Grisham

Publisher:Reginald H. Garrett, Charles M. Grisham

Chapter27: Metabolic Integration And Organ Specialization

Section: Chapter Questions

Problem 20P: Figure 27.3 illustrates the response of R (ATP-regenerating) and U (ATP-utilizing) enzymes to energy...

See similar textbooks

Similar questions

Figure 27.3 illustrates the response of R (ATP-regenerating) and U (ATP-utilizing) enzymes to energy charge. a. Would hexokinase be an R enzyme or a U enzyme? Would glutamine: PRPP amidotransferase, the second enzyme in purine biosynthesis, be an R enzyme or a U enzyme? b. If energy charge = 0.5: Is the activity of hexokinase high or low? Is ribose-5-P pyrophosphokinase activity high or low? c. If energy charge = 0.95: Is the activity of hexokinase high or low? Is ribose-5-P pyrophosphokinase activity high or low?
The enzyme that catalyzes reaction below can be classified as: CoO COO NAD+ NADH + H* Но- | malate -C- H-Ć- dehydrogenase Охaloacetate Malate isomerase lyase hydrolase oxidoreductase ligase transferase
The following reaction is catalyzed by this type of enzyme? Coo COO™ I HIC-H H-C-H COO™ succinate isomerase hydrolase O ligase transferase oxidoreductase succinate dehydrogenase FAD FADH2 H-C || C-H COO fumarate
In step 4 of glycolysis, F16BP is converted to GAP and DHAP. In the mechanism carried out by the aldolase (the enzyme the carries out this reaction) an active site lysine residue reacts with the substrates' carbonyl group to form a Schiff base. Briefly, what is the logic behind the formation of the Schiff base (i.e. why is it beneficial that the enzyme forms this Schiff base)?
The following are coenzymes or cofactors involved in enzymatic reactions. Identify the biochemical role that each plays within a biochemical transformation: Cofactor/Coenzyme Biochemical Role S-adenosylmethionine NADH NADPH FADH2 Biotin Pyridoxal Phosphate Tetrahydrofolate
Aspartate transcarbamoylase, which is necessary for CTP production, is an essential enzyme for the human body. In the below graph, which line represents the rate of the reaction catalyzes by Aspartate transcarbamoylase? Explain.
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 nucleotide
What are the possivble oxidation product of catalase using H2O2 as the substrate? Explain in 1-3 sentences
The Beutler test is used to diagnose GALT (UDP-glucose uridyltransferase) deficiency in infants. Blood from the heel is spotted onto filter paper and the spot is then subjected to an enzyme assay. Galactose 1-phosphate, NADP+ and UDP-glucose are added as substrates to the dried blood. The increase in absorbance at 340nm is measured over time which corresponds to reduction of NADP+ to NADPH . The amount of GALT activity in the blood of patients is therefore measured by stoichiometric relationship to the amount of NADPH produced from NADP+. However, GALT does not directly reduce NADP+ as you can see in the above diagram. Instead, the glucose 1-phosphate product from this reaction is shuttled into the oxidative phase of the pentose phosphate pathway by enzymes also present in RBCs. Which three (or possibly more if you must) enzymes downstream of GALT allow for quantitative correlation of a product of GALT with the appearance of NADPH? What is the stoichiometric relationship…
Below is an image of the Krebs cycle: acetyl-CoA oxaloacetate COASH H20 NADH NAD* H20 malate citrate fumarate isocitrate FADH2 NAD* CO2 FAD АТР NADH + ADP succinate GTP NAD+ a-ketoglutarate H20 GDP NADH + CO2 COASH succinyl CoA COASH Consider the conversion of succinate to fumarate, which is coupled with the production the electron carrier FADH2. If this reaction was NOT coupled with the production of FADH2 (and only catalyzed the conversion of succinate to fumarate), how would this impact ATP production through cell respiration? OATP production would stop because no high energy electron carriers would be produced ATP production would still occur, but there would be a much lower ATP yield because a large number of electron carriers are no longer being made ATP production would stop because without FADH2 we will no longer have electrons moving through the electron transport chain ATP production would still occur, but there would be a slightly lower ATP yield because a small number of…
We talked about the types (mechanisms) of catalysis, including acid-base catalysis, covalent bond formation, metal ion stabilization, and nucleophile attacks of reactants/intermediates following substrate binding. Using the SN2 mechanism for Peptidoglycan cleavage by Lysozyme, indicate the type of catalysis that each of these groups are taking part in. Provide your answers in the thread. Note: this is not part of the assignments for Friday. i. Glu35 ii. Asp52 iii. H2O
There is a cysteine protease, which uses a similar chemical mechanism to chymotrypsin except for using cysteine instead of serine during catalysis. Please draw the stepwise chemical mechanism for the cysteine protease.