Select the following enzymes that utilize a mechanism involving covalent catalysis. Triose phosphate isomerase Glyceraldehyde 3 - Phosphate Dehydrogenase Aldolase Class II Hexokinase Aldolase Class I
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- asapSelect the following enzymes that utlize a mechanism involving covalent catalysis. Select ALL that apply: a) aldolase class 1 b) glyceraldehyde 3 phosphate dehydrogenase c) aldolase class 2 d) triose phosphate isomerase e) hexokinaseCertain microorganisms with a modified citric acid cycle decarboxylate α-ketoglutarate to produce succinate semialdehyde:
- Indicate the general type of enzyme that mediates each glycolysis reaction depicted below. (e.g. Transferase, Oxidoreductase, Kinase, Hydrolase, Lyase, or Isomerase) iii. O H Glyceraldehyde-3-phosphate → 1,3-Bisphosphoglycerate H-C-OH + NAD CH₂O-P + P₁ H-O- -C-H Glucose →→ Glucose-6-phosphate H b 0 OH HO OH H-C- 0 -H HO- H ОН H-C-OH + NADH +H+ CH₂O P P ATP ADP 1 H (P-O- -C- H H HO OH 2-Phosphoglycerate → Phosphoenolpyruvate 0 OH H ОН -O~(P) + HOHYou have a crude lysate sample (CL) containing a mixture of six proteins (1, 2, 3, 4, 5, ẞ- galactosidase), and your goal is to obtain purified ẞ-gal. Some characteristics of these proteins are shown in the table below. Protein Alcohol dehydrogenase Carbonic anhydrase Insulin B chain Phosphorylase B Glutamic dehydrogenase B-galactosidase 45% Concentration of ammonium sulfate (AS) required for precipitation Molecular Weight (kDa) Isoelectric point (pl) 38 3.7 80% 65% 20% 30% 45% 28 4.8 4 5.3 98 6.8 49 9.5 115 5.3 You begin your purification by performing an ammonium sulfate (AS) precipitation. You add the appropriate concentration of AS to your CL sample, incubate overnight at 4°C, then centrifuge to generate a supernatant (AS-S) and pellet (AS-P). What concentration of AS will you use to precipitate Glutamic dehydrogenase? © 20% O 30% 45% 65% 80%how does iodoacetate inhibit glycolysis? explain.
- 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…There is another class of aldolase enzymes known as Class II. These enzymes are found in fungi, algae, and some bacteria. This class differs for Class I in that these enzymes do not have a Lys residue associated with their active sites, but contain a divalent cation (usually Zn2+ or Fe2+) in the active site. Outline a possible mechanism for a Class II aldolase and explain the function of the metal ion in the reaction.Please choose the correct order for the glycolytic intermediates listed below. In any given answer, there may be missing intermediates. fructose 1,6 bisphosphate; glyceraldehyde 3 phosphate; 3 phosphoglycerate; dihydroxyacetone phosphate O glucose; glucose 6 phosphate; pyruvate; phosphoenol pyruvate O glucose 6 phosphate; fructose 6 phosphate; 2 phosphoglycerate; pyruvate O fructose 6 phosphate; glucose 6 phosphate; 3 phosphoglycerate; glyceraldehyde 3 phosphate
- Alpha-ketoglutarate dehydrogenase exhibits feedback inhibition byWhich of the following statements inaccurately describes glutamate dehydrogenase? Glutamate dehydrogenase uses either NAD+ or NADP+ in a redox reaction Glutamate dehydrogenase catalyzes an oxidative deamination reaction Glutamate dehydrogenase equilibrium lies with the reductive amination of glutamate Glutamate dehydrogenase utilizes hydrolysis to release ammonium from an imine intermediateOrder the following TCA cycle metabolites in the order they appear in the cycle. Not all answers will be used. 1 isocitrate [Choose] oxaloacetate fumarate alpha ketogluterate aconitate isocitrate 3 pyruvate glucose 6-phosphate lactate [Choose ] 1 pts Question 2 In the reaction catalyzed by malate dehydrogenase, which of the following molecules is classified as the reduced 2.