select the BEST answerAconitase is most interesting in that it:Can be coded for by 2 different genesO Exists as either a membrane bound or soluble protein depending on intracellular conditionsO Has 2 distinct roles depending on the availability of IronO Can change the AGº' of it's reactionO Is itself an allosteric regulator of the PDH complex

Aconitase is an enzyme involved in the Krebs cycle. It catalyzes the conversion of citrate into…

Answered: select the BEST answer Aconitase is…

Biology 2e

2nd Edition

ISBN:9781947172517

Author:Matthew Douglas, Jung Choi, Mary Ann Clark

Publisher:Matthew Douglas, Jung Choi, Mary Ann Clark

Chapter9: Cell Communication

Section: Chapter Questions

Problem 12RQ: Histamine binds to the H1 G-protein-linked receptor to initiate the itchiness and airway...

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Assessing the Effect of Active-Site Phosphorylation on Enzyme Activity (Integrates with Chapter 15.) The serine residue of isocitrate dehydroenase that is phosphorylated by protein kinase lies within the active site of the enzyme. This situation contrasts with most other examples of coa1ent modification by protein phosphorylation. where the phosphorylation occurs at a sate remote from the active site. What direct effect do you think such active-site phosphorylation might have on the catalytic activity of isocitrate dehydrogcn.ise? (Sec Barford, D., 1991. Molecular mechanisms for the control of enzymic activity by protein phosphorytation. Biochimica et Biophysica Acta 1133:55â€”62.)
Provide a diagram of the EPH RECEPTOR B2 (EPHB2) structure. Give annotations of binding sites and enzyme active sites.
Epinephrine causes a liver cell to produce glucose from glycogen in a flight-or-fight response. In the signaling pathway triggered by the specific receptor binding, explain the mechanism for activation of Protein kinase A (PKA). indicate what mechanism/s for enzyme regulation is/are involved in the process (focus on the activation of PKA in response to epinephrine and draw what happens to the enzyme ie how it becomes activated).
Please refer to the model, the answer may be brief.. thank you so much for answering both... i appreciate it1. Explain the mechanism of action of the adenyl cyclic system using a schematic diagram. 2. Cite a metabolic pathway where active protein kinase is needed and explain its mechanism of action
A fixed amount of radiolabelled insulin was incubated with a fixed amount of anti-insulin antibody, the bound ligand was separated from free ligand at different time intervals. Draw a diagram of the concentration of the insulin/antibody complex with time. (Insulin/antibody complex is the bound ligand) asap typed only .
4. Hexokinase is kinase that catalyzes the phosphorylation of glucose by ATP to glucose-6-P, which can bind toits active site, blocking the access to ATP. Which of the following statements is/are correct regarding the typeof regulation?a) Phosphorylationb) Dephosphorylation.c) Feedback inhibition.d) Repression Explain each of the following option
1a. Contrast the activation of cytokine receptors to the activation of receptor threonine kinases. b. We discovered a new cytokine that stimulates cancer cell growth. Now we want to determine if the JAK/STAT pathway is activated after stimulation. In the lab we have a small molecule that can competitively bind to SH2 domains. Explain where and how in the pathway this inhibitor would be effective.
CTP inhibits ATCase; however, the inhibition is not complete. Can you suggest another molecule that might enhance the inhibition of ATCase?
Sketch the arrow pushing mechanism for the acid base catalyzed formation of phospho-serine from protein kinase a. You may shorthand the emzyme, the ribose and the adenine ring in ATP
A female neonate did well until approximately 24 hours of age when she became lethargic. A sepsis workup proved negative. At 56 hours, she started showing focal seizure activity. The plasma ammonia level was found to be 1,100 μmol/L (normal 5–35 μmol/L). Quantitative plasma amino acid levels revealed a marked elevation of argininosuccinate.19.3 Which one of the following enzymic activities is most likely to be deficient in this patient? EXPLAIN your answerA. Arginase.B. Argininosuccinate lyase.C. Argininosuccinate synthase.D. Carbamoyl phosphate synthetase I.E. Ornithine transcarbamoylase.
The epinephrine-mediated “amplificationcascade” of Figure 24.14 has six steps, all of which are catalyticwith one exception. This cascade leads to the activation of glycogenphosphorylase. This enzyme acts in turn on glycogen to yieldglucose-1-phosphate (G-1-P).(a) Which step is not catalytic?(b) If each catalytic step had a turnover (molecules of substrateacted on per molecule of enzyme) of 10, how many moleculesof G-1-P would result from one molecule of epinephrine?(c) What is the biochemical advantage of such a cascade?(d) How is the amplification cascade of this questionreversed?
In the lungs what is the occurring with respect to the [H+] of the microenvironment of the red blood cells to aid in oxygen transport? Select all that apply BPG binding causes the release of protons from the central cavity of the R-state that favors quaternary shift to the T-state Carbamates are forming, causing ionization of protons that leads to [H+] decrease and stabilization of oxygenated Hb Large amounts of bicarbonate being produced, leads to a decrease in pH and stabilization of the T-state of Hb Bicarbonate is picking up protons from Hb as it transtions to the R-state, combating the decrease in the [H+] Carbonic anhydrase is catalyzing a reaction that consume protons, thus Hb is ionizing protons to help prevent change in pH

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