Part A N- N. Which of the following is found in the coenzyme FAD? IN Check all that apply. two heteracyclic tings ADP HO a substituted benzene ring HO HO a phosphate anhydride bond
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- NH3 gala. S Co A C H₂ R-C S CH₂ HN ĐÌNH ΝΗ CH₂ CH₂ NH 3. Compare and contrast how thiolase and chymotrypsin creates and stabilizes its intermediates.His388 Glu357 His388 Glu357 Ring opening Proton HO HO abstraction HO но- G6P He NH- NH His388 His388 His388 Glu357 Glu357 Glu357 HO но HO но- но OH cis-enediol F6P Ring closure intermediate OH Describe the mechanism shown above for phosphoglucose isomerase. Describe the chemistry of each step • How the enzyme appears or might facilitate the chemistry How the enzyme increases the reaction rate.What is the catalytic efficiency of Catalase ? Table. The values of KM and kcat for some Enzymes and Substrates Enzyme Carbonic anhydrase Substrate CO2 HCO3 KM (M) 1.2 x 10-2 2.6 x 10-2 Kcat (s-1) 1.0 x 106 4.0 x 105 Catalase H2O2 2.5 x 10-2 1.0 x 107 Urease Urea 2.5 x 10-2 4.0 x 105 O A. 4 x 108 M-s-1 O B. 4 x 108 M-1.s-1 OC25x 10-9 M-s1 D. 2.5 x 102 M-1.s-1 OE 1.0 x 107 s1
- nfile.php/7382360/mod_resource/content/0/Pyrimidine%20Practice%20Pat 1 / 1 67% + | 田 Pyrimidine Synthesis El * be surc to label reguletary Steps K carbamay1 phiuphate E2 orotate R-5P Eg UMP d TMP ATP ADPEE3 TET EedUDP O dumP E4 E5 CTP-> dCDPHO-C-CH,-CH,~ Identify the enzyme needed in each of the following reactions as an isomerase, a decarboxylase, a dehydrogenase, a protease, or a phosphatase. о CH;-C-Č-OH → CH;-Č–H + CO, СНО CH,OH НС—ОН C=0 HO-CH — НО -СН НС—ОН НС—ОН HO-CH Но -СH CH-OPO,?- ČH-OPO,- Но -С—СН,—CH, —С—ОН — Но -С—СН—СH-С-ОН + 2Н H;N-CH-C-NH-CH-CO0 +H;O → CH; ČH3 2 H;N-CH-CO0- ČH3QUESTION 3 Bioremediation is a branch of biotechnology that employs the use of living organisms to remove toxic substances; such as, mercury, radioactive material, industrial waste, and the petroleum products of oil spills from the water and soil in our environment. Here is a figure that shows the bacterial degradation of the poly-aromatic hydrocarbon, naphthalene. In this figure showing the catabolic metabolism of naphthalene, would you predict the metabolites catechol, salicylate, and gentisate generated in this process to (select one): Proposed catabolic pathways of naphthalene by bacteria 1,2-Naphthoquinone Coumarin Catechol OH OHL 35-8-8-8-8 OH OH Naphthalene cis-1,2-Dihydroxy- 1,2-dihydronaphthalene 1,2-Dihydroxynaphthalene O COOH OH 2-Hydroxy-2H-chromene- 2-carboxylic acid cis-o-Hydroxybenzalpyruvate COOH 2-Hydroxybenzaldehyde OH Gentisate COOH
- H,N. NH3 HO, H,O H,N. NH2 COOH СООН glutamic acid glutamine why does the reaction not proceed?NH3 H-SCO A LES NH CH₂ NH CH₂ CH₂ 3 H-SCO A H3C SCO A 5. Describe the role of His in the catalytic mechanism shown.I lea the - Oligopeptide 2 a. Give the three-letter and one-letter names of the amino acids in each oligopeptide starting from the amino terminal to the carboxyl terminal. Make sure that the amino acid names are arranged in CORRECT order for both oligopeptides. I b. After complete hydrolysis, which oligopeptide will yield more ATP molecules? How many NADH and FADH2 molecules will be theoretically produced? Show all relevant computations for each oligopeptide. Tabulate your answers to keep your answers organized. ( Oligopeptide Net ATP molecules Net NADH produced Net FADH2 produced produced Oligopeptide 1 Oligopeptide 2
- 困 1 Which amino acid group is attributed Tryptophan could be considered as 'to the Maple syrup urine disease as 2 precursor of which compound? * Most of the ammonia released from 3 What cofactor is required for the 4 Which of following statements about 1 alpha amino acids reflects the Isynthesis of amino acid from carbohydrate intermediates in 5 hydroxyproline is INCORRECT? * an inborn error of metabolism? coupled action of transaminase and Melanin what other catalyst? * transamination? * Hydroxylation of proline residues is catalysed by a dioxygenase. Dicarboxylic amino acids O Melatonin O L-glutamate dehydrogenase O Niacin O Aromatic amino acids O Epinephrine Free proline cannot be hydroxylated to hydroxyproline. O L-amino acid oxidase Thiamin O Branched chain amino acids O Thyroid hormones O Carboxylase O Pyridoxal phosphate It is present in large amounts in collagen Sulphur-containing amino acids O Aminotransferase O There is no codon for hydroxyproline. O Riboflavin 7 Which of the…R HO OH OH H₂N CH3 protein asparagine side chain activated sugar Draw the product of the asparagine glycosylation reaction, assuming inversion of configuration of the anomeric carbon.S 1 CH₂ ✪ NH3 0=0 H₂C HN 6 NH CH₂ 'S Co A L CH₂ NH 4. Describe the role of His in the catalytic mechanism shown.
