The degradation of CH3 (CH₂ )10 - COOH via the beta-oxidation pathway requires: 6FAD + 6NAD+ + 5C0A-SH+ 6H₂O 5FAD + 5NAD+ + 6C0A-SH+ 5H₂O 5FAD + 5NAD+ + 5C0A-SH+ 5H₂0 6FAD + 6NAD+ + 6C0A-SH + 6H₂O
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- Write out the balanced chemical equation for the FIRST round of oxidation of C16:cis-9.Copper is a cofactor in several enzymes, including lysyl oxidase and superoxide dismutase.Ceruloplasmin, a deep-blue glycoprotein, is the principal copper-containing protein in blood. It isused to transport Cu2+ and maintain appropriate levels of Cu2+ in the body’s tissues.Ceruloplasmin also catalyzes the oxidation of Fe2+ to Fe3+, an important reaction in ironmetabolism. Because the metal is widely found in foods, copper deficiency is rare in humans.Deficiency symptoms include anemia, leukopenia (reduction in blood levels of white blood cells),bone defects, and weakened arterial walls. The body is partially protected from exposure toexcessive copper (and several other metals) by metallothionein, a small, metal-binding protein thatpossesses a large proportion of cysteine residues. Certain metals (most notably zinc and cadmium)induce the synthesis of metallothionein in the intestine and liver.In Menkes syndrome intestinal absorption of copper is defective. How can affected infants…Draw the products of the reaction of xylulose-5-phosphate and erythrose-4-phosphate catalyzed by transketolase in the pentose phosphate pathway. Provide the structure in the protonation state found in physiological conditions. H H H OH FO HO-H H-OH H OPO3²- Q transketolase Draw glyceraldehyde-3- phosphate H H- H H H O OH OH OPO3²- Draw fructose-6- phosphate Q I I
- Which of the following statements is true about the chymotrypsin reaction? 1. The catalytic triad at the active site is formed by three residues: His, Gly, and Ser 2. When the substrate is p-Nitrophenylacetate, the rate-limiting step is the release of p-Nitrophenolate. 3. During the reaction, LBHB forms when the proton is donated to His from Ser or water. 4. The chymotrypsin reaction involves “only” specific acid-base catalysis 5. The “oxyanion hole” is formed by the amide nitrogens of Ser and GluUnder anaerobic conditions, Escherichia coli synthesizes an NADH-dependent fumarate reductase rather than succinatedehydrogenase, the flavoprotein that oxidizes succinate to fumarate. a) Write an equation for the reaction catalyzed by fumarate reductase.b) NADH produced by the glyceraldehyde-3-phosphate dehydrogenase reaction is re-oxidized by reducing an organicintermediate. Rather than reduce pyruvate to lactate, anaerobic E. coli utilize fumarate reductase. However, underanaerobiosis, the activity of -ketoglutarate dehydrogenase is virtually nonexistent. Show how fumarate is formed, usinga reaction beginning with PEP and including the necessary TCA cycle enzymes.c) What is the metabolic advantage to anaerobic E. coli in using the fumarate reductase pathway rather than lactatedehydrogenase to re-oxidize NADH?One process catalyzed by NADHNADH dehydrogenase is NADH+H^++ubiquinone ↽−−⇀ NAD+ubiquinolNADH+H^++ubiquinone ↽−−⇀ NAD^++ubiquinol The standard reduction potentials for the half‑reactions are given in the table. Oxidant Reductant ?′0 ubiquinone+2H++2e−ubiquinone+2H++2e^− ubiquinolubiquinol 0.045 NAD^++H^++2e−NAD^++H^++2e^− NADHNADH –0.32 Calculate Δ?′0 for the reaction as shown. Δ?′0=____(V) Calculate Δ?′0 . Δ?′0=____(kJ/mol)
- Which cytochrome P450-catalyzed reaction is shown below? R-CH2NH2 [R-CH=NH] Oxidation of aromatic amines Oxidative deamination Oxidative O-dealkylation Oxidative N-dealkylation para-hydroxylation R-CHO + NH3The mechanism involved in the reaction catalyzed by phosphoglyceromutase is known to involve a phosphorylatedenzyme intermediate. If 3-phosphoglycerate is radioactively labeledwith 32P, the product of the reaction, 2-phosphoglycerate, does nothave any radioactive label. Design a mechanism to explain these facts.Propose a mechanism for the Co2 + catalyzed hydrolysis of glycinamide.
- [1-14C]Ribose 5-phosphate is incubated with a mixture of purified transketolase, transaldolase, phosphopentose isomerase, phosphopentose epimerase, and glyceraldehyde 3-phosphate. Predict the distribution of radioactivity in the erythrose 4-phosphate and fructose 6-phosphate that were formed in this system. Diagram the reactions involved, showing the structures of each intermediate compound in the system and clearly indicating the location of the 14C in each molecule.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.Consider the mechanism of enolase, as indicated below. Which of the following correctly describes the roles of the Mg2+ as illustrated in the figure? (This is a multi- select question). Mg2+ Mg2 Enolase PO3- OH -C-C-H H OH HO H-N-H Lys 345 Glu211 2-Phosphoglycerate bound to enzyme Mg2+ Mg2 PO3- OH C-C-H OH HO H H-N*-H Lys 345 O Glu211 Enolic intermediate HOH PO3- H Phosphoenolpyruvate The metal ion (Mg2+) is helping to stabilize the extra negative charge that developed on the carboxyl group in the enolic intermediate. The metal ion (Mg2+) is serving as a general base, removing a proton in order to improve the quality of the nucleophile. The metal ion (Mg2+) is assisting in the oxidation of the carboxyl carbon through metal ion catalysis. The metal ion (Mg2+) is helping to orient the substrate properly in the active site. The metal ion (Mg2+) is accepting a proton in order to improve the quality of the leaving group.