A new mutation in Saccharomyces cerevisiae, a eukaryotic yeast, causes the cells to be unable to produce adequate amounts of enzyme ERF5, Upon examination, the ERF5 enzyme in the mutant yeast is exactly the same as the wild type except for the reduced levels in the ERFS mutant. Explain the mutation.

A new mutation in Saccharomyces cerevisiae, a eukaryotic yeast, causes the cells to be unable to produce adequate amounts of enzyme ERF5, Upon examination, the ERF5 enzyme in the mutant yeast is exactly the same as the wild type except for the reduced levels in the ERFS mutant. Explain the mutation.

Biochemistry

6th Edition

ISBN:9781305577206

Author:Reginald H. Garrett, Charles M. Grisham

Publisher:Reginald H. Garrett, Charles M. Grisham

Chapter19: The Tricarboxylic Acid Cycle

Section: Chapter Questions

Problem 20P

See similar textbooks

Similar questions

Need help Sesamin is one of the major lignans found in sesame oil. Sesamin-metabolic pathways remain uncharacterized at both the enzyme and gene levels. However, one microorganism showed significant sesamin-degrading activity and was identified as Sinomonas sp. no. 22. A sesamin- metabolizing enzyme named SesA was purified from this strain and characterized. Explain how sesamin methylene transferase was identified and characterized and explain the mechanism. Based on your knowledge, what other assays could be run to characterize this enzyme?
in human 2. Human xanthine oxidase catalyzes the oxidation of hypoxanthine to xanthine and can further catalyze the oxidation of xanthine to uric acid. For the treatment of hyperuricemia and gout. several medications are used to inhibit the activity of xanthine oxidase and reduce the production of uric acid. You are a biochemist and just discovered a chemical that can inhibit the activity of the human xanthine oxidase. When analyzing its mode of inhibition, you found that the enzyme inhibitor complex requires 450 kJ.mol to dissociate and that it displays kinetics somehow similar to noncompetitive inhibition. You sent your inhibitor to the ministry of health for approval as a medication for gout. Based on the data provided, are they going to authorize it as a medication or not? Explain?
АСTIVITY For each of the 4 regulatory states of the lac shown in the following diagram, answer the following questions: оperon 1) Is glucose present? 2) Is lactose present? Synthesis of lac MRNA? Glucose present? Lactose present? NO Repressor y a NO CAMP-CRP complex y YES Transcription i p o y NO
Molecular detail of spike Y453F
8 of 15 An enzvme has an all-important histidine residue in its active site such that substitution with an other amino acid would result to the loss of catalytic activity. What are the possible mechanisms by which this histidine residue may facilitate catalysis? I. Acting as proton acceptor. II. Forming of covalent bond with the substrate via an ester bond. III. Serve as stabilizer of electrophilic substrate because of its nucleophilic character. Select the correct response: land II Il and III land IlI I. Il, and III
10-¹1 M. A 1 nM (10-⁹ M) solution of lysozyme is o An Fab fragment binds to lysozyme with a dissociation constant of Kå treated with increasing concentrations of the Fab fragment. At what concentration of added Fab will half of the lysozyme be bound to the Fab? [F] = nM
A. Lineweaver-Burk plot of the enzyme with increasing amounts of substrate in the absence or the presence of the inhibitor is shown below. Graph A : x-intercept Graph B : x-intercept = - 0.012, y-intercept = 0.8 Graph C : x-intercept = - 0.027, y-intercept = 0.8 Graph D : x-intercept = - 0.039, y-intercept = 0.8 - 0.007, y-intercept = 0.8 Graph A 4 Graph B Graph C Graph D 1 -0,04 -0,02 0,00 0,02 0,04 1/[Substrate] (uM) (i) Which graph indicates an enzymatic reaction without inhibitor? (ii) Which type of inhibitor is it? Briefly explain. (iii) Which graph indicates the highest concentration of inhibitor? (iv) Calculate the Vmax and Km of the graph showing an enzymatic reaction with the lowest concentration of inhibitor. Show the steps of calculation and unit in your answers. Keep 2 decimal places in your answers. 1/Rate (umol/min)
Plz answer correctly do not copy. Question- 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
Fill in the blanks (write answers only in correct sequence). When the activation energy required is less between the reactants and the products, reaction is known as----- i. ii. The region of an enzyme where substrate molecules bind and undergo a chemical 11. reaction is known as--- 11. To produce amino acids and synthesis of NADH, cycle used is-- Metabolic cycle that takes place both in cytoplasm and mitochondria is--- Glucose 1 phosphate is converted to Glucose 6 Phosphate by the action of - Which vitamin deficiency is linked with the night blindness? Name it iv. V. vi.
Variant 2 1. Using the structure of d-TMP show all the structural fragments donated by different organic compounds during d-TMP synthesis (in the structure each fragment must be shown using arrow directed from the donor's name). 2. Reasons for hyperuricemia state in humans and its diagnostics.
Genetic control O The product of a series of reactions acts as an inhibitor for an earlier reaction. O Hormones control the synthesis of enzymes. A regulator binds to the enzyme at a site other than the active site. This binding changes the shape of the enzyme and alters the catalytic ability of the enzyme. An inhibitor binds reversibly to the enzymesubstrate complex, blocking the binding of the second substrate to the active site. The activity of an enzyme is influenced by the addition or removal of a group that is covalently bonded to the enzyme. An inhibitor forms covalent bonds to the active site, permanently blocking it.
aestion How does myoglobin minimize oxidation of the Fe(II) when the heme binds to oxygen? Select one: a. the distal His E7 forms a hydrogen bond to the bound molecular oxygen O b. the oxygen binding site is buried in the hydrophobic core away from water O c. the proximal His F8 forms a coordinate bond to Fe(II), which inhibits oxidation O d. nonpolar interactions with residues Val E11 and Phe CD1 limit oxidation by oxygen Oe. the heme shifts to a planar structure that traps iron in a +2 oxidation state Clear my choice