Concept explainers
To determine: The way in which regulatory enzymes can be influenced by reversible covalent modification.
Introduction: The
To determine: The group that is used for reversible covalent modification with glutamine synthetase and the form of the active enzyme.
Introduction: The metabolic pathway can be altered by the direct inhibition or stimulation of the “critical enzyme” activities. Such regulation is posttranslational regulation because it occurs after the synthesis of the enzyme. Covalent modification, cleavage of the protein, and allosteric regulation are some mechanisms of posttranslational regulation.
Want to see the full answer?
Check out a sample textbook solutionChapter 10 Solutions
Prescott's Microbiology
- Amino transferases catalyze the transfer of amino groups to alpha-keto acids with pyridoxal phosphate as the prosthetic group. Pyridoxal phosphate can accept an amino group, and its aminated form, pyridoxamine phosphate, can donate its amino group to an alpha-keto acid. Draw the detailed mechanism of the transamination reaction in the active site of an aminotransferase. Use the glutamate oxaloacetate transaminase as an example.arrow_forwardmTOR is a cytoplasmic kinase that regulates cell division. Its misregulation can lead to cancer. The canonical mTOR inhibitor, rapamycin, is FDA approved as a cancer treatment. Rapamycin is an allosteric inhibitor that does not bind anywhere near the substrate binding site of the enzyme. A) What is the name of this type of inhibition? B) Sketch a REPRESENTATIVE double-reciprocal/Lineweaver-Burke plot that includes the enzyme kinetics for BOTH the uninhibited and inhibited reaction. Be sure to: 1) Make ABSOLUTELY clear which curve is your uninhibited reaction and which is your inhibited reaction. 2) Label the X and Y axes. 3) Indicate what the X- and Y-intercepts represent with regards to Michaelis-Menten kinetics. C) Can increasing the substrate concentration overcome this type of inhibition? Explain in a sentence or two.arrow_forwardWhy is it advantageous for two control mechanisms —allosteric control and covalent modification— to be involved in the metabolism of glycogen?arrow_forward
- Azaserine inhibits amidotransferases. State the purine precursor that resembles azaserine. Which step in the purine biosynthetic pathway will be inhibited?arrow_forwardDraw a mechanism using the general features of a serine protease to explain how inhibitor x might work using the following information: inhibitor x is a representative of a new family of serine protease inhibitors. treatment of chymotrypsin with inhibitor X rapidly decreased activity. to determine the mode of inhibition the researchers used dialysis to exchange the buffer with buffer lacking free inhibitor x. after dialysis, the enzyme did NOT recover any activity.arrow_forwardAmino transferases catalyze the transfer of amino groups to alpha-keto acids with pyridoxal phosphate as the prosthetic group. Pyridoxal phosphate can accept an amino group, and its aminated form, pyridoxamine phosphate, can donate its amino group to an alpha-keto acid. Illustrate the detailed mechanism of the transamination reaction in the active site of an aminotransferase. Use the glutamate oxaloacetate transaminase as an example.arrow_forward
- Chymotrypsin, trypsin, and elastase all share the same catalytic mechanism, but have different specificities. (a) These proteases are considered serine proteases because the active sites contain serine, histidine and aspartate. Describe the roles that each of these amino acid residues play in hydrolyzing protein substrates. (b) The active site pockets of chymotrypsin, trypsin, and elastase are shown in the image below. Based on the image, which side chain of the amino acids would they prefer to cleave respectively, Ala, Arg, or Trp? Explain your answers. Val 216KVal 190 Asp 189 Chymotrypsin Trypsin Elastasearrow_forwardChymotrypsin, trypsin, and elastase all share the same catalytic mechanism, but have different specificities. (a) These proteases are considered serine proteases because the active sites contain serine, histidine and aspartate. Describe the roles that each of these amino acid residues play in hydrolyzing protein substrates. (b) The active site pockets of chymotrypsin, trypsin, and elastase are shown in the image below. Based on the image, which side chain of the amino acids would they prefer to cleave respectively, Ala, Arg, or Trp? Explain your answers. Val 216 Val 190 Asp 189 Chymotrypsin Trypsin Elastasearrow_forwardUDP-glucuronosyltransferase enzymes bind the organic compound UDP-glucuronic acid (UDP-GA) in order to catalyse the transfer of a glucuronic acid group from UDP-GA to a drug molecule, releasing UDP from the active site as a product. UDP is then regenerated by the activity of another enzyme. What terms could be used to describe UDP-GA?arrow_forward
- Why is penicillin such an effective inhibitor of the transpeptidase?arrow_forwardHow is carbamoyl-phosphate synthetase I (CPS-I) controlled?arrow_forwardThe M and H subunits of lactate dehydrogenase have very similar sizes and shapes but differ in amino acidcomposition. If the only difference between the two were that theH subunit had a glutamic acid in a position where the M subunithad a serine, how would the five isozymes of LDH separate on electrophoresis using a gel at pH 8.6?arrow_forward
- Human Anatomy & Physiology (11th Edition)BiologyISBN:9780134580999Author:Elaine N. Marieb, Katja N. HoehnPublisher:PEARSONBiology 2eBiologyISBN:9781947172517Author:Matthew Douglas, Jung Choi, Mary Ann ClarkPublisher:OpenStaxAnatomy & PhysiologyBiologyISBN:9781259398629Author:McKinley, Michael P., O'loughlin, Valerie Dean, Bidle, Theresa StouterPublisher:Mcgraw Hill Education,
- Molecular Biology of the Cell (Sixth Edition)BiologyISBN:9780815344322Author:Bruce Alberts, Alexander D. Johnson, Julian Lewis, David Morgan, Martin Raff, Keith Roberts, Peter WalterPublisher:W. W. Norton & CompanyLaboratory Manual For Human Anatomy & PhysiologyBiologyISBN:9781260159363Author:Martin, Terry R., Prentice-craver, CynthiaPublisher:McGraw-Hill Publishing Co.Inquiry Into Life (16th Edition)BiologyISBN:9781260231700Author:Sylvia S. Mader, Michael WindelspechtPublisher:McGraw Hill Education