Arsinate binds to reduced thio groups such as those found in cystiene residues in proteins, lipoate or glutathione. The resulting inhibition leads to central nervous system pathologies. The binding of arsinate to the dihydrolipoyl groups inhibits which of the following enzyme(s)? succinate dehydrogenase malate dehydrogenase pyruvate dehydrogenase complex branched-chain amino acid dehydrogenase complex isocitrate dehydrogenase alpha-ketoglutarate dehydrogenase complex

Arsinate binds to reduced thio groups such as those found in cystiene residues in proteins, lipoate or glutathione. The resulting inhibition leads to central nervous system pathologies. The binding of arsinate to the dihydrolipoyl groups inhibits which of the following enzyme(s)? succinate dehydrogenase malate dehydrogenase pyruvate dehydrogenase complex branched-chain amino acid dehydrogenase complex isocitrate dehydrogenase alpha-ketoglutarate dehydrogenase complex

Biochemistry

6th Edition

ISBN:9781305577206

Author:Reginald H. Garrett, Charles M. Grisham

Publisher:Reginald H. Garrett, Charles M. Grisham

Chapter26: Synthesis And Degradation Of Nucleotides

Section: Chapter Questions

Problem 16P

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Please answer fast Arsinate binds to reduced thio groups such as those found in cystiene residues in proteins, lipoate or glutathione. The resulting inhibition leads to central nervous system pathologies. The binding of arsinate to the dihydrolipoyl groups inhibits which of the following enzyme(s)? a.succinate dehydrogenase b.malate dehydrogenase c.pyruvate dehydrogenase complex d.branched-chain amino acid dehydrogenase complex e.isocitrate dehydrogenase f.alpha-ketoglutarate dehydrogenase complex A common and effective treatment for arsenite poisoning involves administration of _____. a.aresenite chelator b.vitamin B1 c.a competitive sulfhydryl reagent d.NADPH e.a dihydrolipoyl inhibitor
What is the effect of the following mutations of succinate Dehydrogenase/Complex II? Would you expect them to cause the catalytic activity to increase, decrease or stay about the same? First explain the normal function of the amino acid side chain listed, then how the structure of the mutant is different and then how that would lead to your choice of increase, decrease or stay about the same. Be sure to use the specific structures of the amino acid side chains in your answers. a) His99Phe b) Arg297unusual AA below
Using the word anomeric carbon, “acceptor” nucleophilic substrate, and activated “donor”, describe how Glycosyl transferase's (and glycosidases) catalyze glycan and glycoconjugate formation Please answer asap
There are parts A-C for this picture included. A) What type of enzyme is Malate Dehydrogenase? choices: Hydrolase, Isomerase, Ligase, Oxideoreductase, Transferase, or Translocase B) Which of the following statements are true in biochemical standard conditions? There can be more than 1. Choices: The reaction is spontaneous since ∆G°' is positive The reaction is spontaneous since ∆G°' is negative The reaction is not spontaneous since ∆G°' is positive The reaction is not spontaneous since ∆G°' is positive The equilibrium favors products since K is greater than 1 The equilibrium favors reactants since K is greater than 1 The equilibrium favors products since K is less than 1 The equilibrium favors reactants since K is less than 1 The reaction is always at equilibrium C) If the concentration of Oxaloacetate is 10^7 times lower than the concentration of Malate D.,Is the reaction Spontanuous? Choices: No, because RTInQ is very positive Yes, because RTlnQ is very…
Legend: Blue – wild-type β-galactosidase Red – mutant β-galactosidase _________ a. What is the optimum pH of wild type β-galactosidase? _________ b. What is the optimum temperature of mutant β-galactosidase? _________ c. Which enzyme has the greater activity at pH 7.2? _________ d. Which enzyme has the greater activity at a temperature of 42.5oC? _________ e. Which enzyme has greater activity if pH decreases from 7.5 to 6.4? _________ f. Which enzyme has greater activity if temperature increases from 40oC to 41 oC?
Please answer I will give you like Dwarfism was found to be a result of the overproduction of Enzyme X that deactivates the growth hormone. Initial fractionation using Sephadex G-100, a molecular sieve, was done, followed by subsequent purification steps until a pure form of Enzyme X was obtained. Part of the study on Enzyme X was the determination of its primary structure. Because of its big size, Enzyme X was cut into smaller peptides by treatment of enzymes and cyanogen bromide. One of the fragments was hydrolyzed and the amino acid components were separated by ion-exchange chromatography and identified. The amino acids were found to be: arg, asp, ile, lys, met, and tyr. The sequence was determined as follows: Treatment with DNFB gave a mixture of amino acids and DNP-lys Treatment with trypsin gave an amino acid, a dipeptide and a tripeptide ; the tripeptide tested positive with the Sakaguchi test Treatment with CNBr gave two tripeptides Treatment with chymotrypsin gave a…
Please solve all part. 9. If 32p-labeled inorganic phosphate were introduced to erythrocytes undergoing glycolysis which of the following molecules would you NOT expect to detect 32p in? ** Multiple answers: Multiple answers are accepted for this question a. Fructose 1-6 bisphosphate b. 3-Phosphoglyceraldehyde c. Dihydroxyacetone phosphate d. 2-Phosphoglycerate e. 1-3 bisphosphoglycerate f. Phosphoenolpyruvate g. 3-Phosphoglycerate h. Pyruvate i. Glucose 6-Phosphate
Trypsin contains a/an [aspartate/serine/histidine] in its specificity pocket to attract lysine and arginine side chains. It contains a potent nucleophilic [histidine/serine/aspartate] in its active site that is capable of attacking the electrophilic [carbon/nitrogen/oxygen] of the closest peptide bond. The [acyl-enzyme/specificity pocket/oxyanion] transition state is stabilized by the backbone amide hydrogens of glycine and serine. In this way, the enzyme is able to catalyze the [hydrolysis/ligation/metalysis/hydrogenation] of the peptide bond.
Lactate dehydrogenase is a tetramer of MW 134000 g/mole composed of subunits which are equal in size. It is found in the cytoplasm of eukaryotic and prokaryotic cells. Describe the secondary, tertiary and quaternary structures of lactate dehydrogenase.
Kindly answer numbers 15, 16, and 17 13. A 10-year old boy was evaluated for burning sensations in his feet and cluster of small, red- purple spots on his skin. Laboratory studies revealed protein in his urine. Enzymatic analysis revealed a deficiency of α-galactosidase, and enzyme replacement therapy was recommended. The most like diagnosis is:a. Fabry diseaseb. Farber diseasec. Gaucher diseased. Krabbe disease 14. What possible sphingoglycolipids will accumulate from the enzyme deficiency mentionedin number 13?a. Sulfatidesb. Globosidesc. Gangliosidesd. Glucocerebrosides15. What is the structural feature of the accumulated membrane lipids involve in the casenumber 13 and 14?a. Sphingosine + FA + cholineb. Sphingosine + 1FA + glucosec. Sphingosine + 1FA + oligosaccharided. Glycerol + 2FA + Phosphate + ethanolamine16. Glycophospholipid that is associated with lung surfactanta. Phosphatidylethanolamineb. Phosphatidylinositolc. Phosphatidylcholined. Phosphatidylserine17. Based on…
Chart is Given for you: Below is a chart of values for actual enzymes. Enzyme Km (M) kcat (1/s)Chymotrypsin 1.5 × 10^−2 0.14Pepsin 3.0 × 10^−4 0.5Tyrosyl-tRNA synthetase 9.0 × 10^−4 7.6Ribonuclease 7.9 × 10^−3 7.9 × 10^2Carbonic anhydrase 2.6 × 10^−2 4.0 × 10^5Fumarase 5.0 × 10^−6 8.0 × 10^2 Assume the enzyme concentration is equal across all samples (and is equal to 1). (Answer a and b only)a. Which enzyme will have the highest V0 at very high substrate concentrations? (1 M). Why? b. Which will have the highest V0 at very low substrate concentrations (5.0 × 10^−12). Why?
can somone please List the components of the enzyme complex involved in the transition step and Simply describe what does each component does? 1. 2. 3. ect..