Biochemistry
9th Edition
ISBN: 9781319114671
Author: Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher: W. H. Freeman
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a protease that cleave peptide bonds adjacent to aspartate and glutamate would likely have an s1 pocket that contain positively charged amino acids
true or false
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- Many enzymes are switched "on" by attachment of a phosphate group at a specific serine somewhere on the protein (phosphorylation). The basic reaction is: E + ATP2 Ep + ADP Po SERINE PHOSPHO SERINC (Note the "squiggles" before the backone amide and carbonyl indicate the polypeptide chain continues on either side of the serine). For phosphorylation to have this effect, there has to be some equilibrium between inactive and active forms conformations of the enzyme: [Eactive] [Einactive] Einactive 2 Eactive; K* The same basic equilibrium must exist for the phosphorylated protein: [Ep,active] [Ep,inactive] EP,inactive 2 Ep,active; Kp = (a) If phosphorylation increases the measured activity of the enzyme, is K* or K larger? Why? (b) Does the phosphorylation site need to be near the site where the enzyme binds its substrate (e.g. the reactant whose chemistry it catalyzes)? Why or why not?arrow_forward"Binding of extracellular ligands to receptor tyrosine kinases (RTKs) activates the intracellular catalytic domain by propagating a conformational change across the lipid bilayer through a single transmembrane a helix" is true or false.arrow_forwardInsulin resistance, as occurs in type 2 diabetes, may lead to increased ketone production and release into blood. Describe the biochemistry that links insulin resistance and ketone production. Compare the cellular energy (e.g. ATP) required and produced when glycogen is synthesize and hydrolyzed, respectively. Compare and contrast the mechanism of fatty acid synthase with translation. When young rats are placed on a totally fat acid free diet, they grow poorly, develop a scaly dermatitis, lose hair, and soon die these symptoms that can be prevented if plant material is included in the diet. Why?arrow_forward
- The hexokinases are a class of enzymes that catalyze the ATP-dependent phosphorylation of hexoses (sugars with six carbons). The hexokinases will bind only D-hexose sugars and not their L-counterparts. In general terms, describe the features of enzyme structure that make this specificity possible.arrow_forwardThe venom of the Eastern diamondback rattler and the Indian cobra contains phospholipase A2, which catalyzes the hydrolysis of fatty acids at the C-2 position of glycerophospholipids. The phospholipid breakdownproduct of this reaction is lysolecithin (lecithin is phosphatidylcholine). At high concentrations, this and other lysophospholipids act as detergents, dissolving the membranes of erythrocytes and lysing the cells. Extensive hemolysis may be lifethreatening.(a) All detergents are amphipathic. What are the hydrophilic and hydrophobic portions of lysolecithin?(b) The pain and inflammation caused by a snake bite can be treated with certain steroids. What is the basis of this treatment?(c) Though the high levels of phospholipase A2 in venom can be deadly, this enzyme is necessary for a variety of normal metabolic processes. What are these processes?arrow_forwardThe enzyme phosphoglucomutase interconverts glucose-1-phosphate and glucose-6-phosphate. Why is this enzyme likely to include a side chain such as Ser in its active site?arrow_forward
- To answer this question, please reference the Problem Solving Video: pH and pK, of an Amino Acid. Proteases are enzymes that cleave peptide bonds using general acid-base catalysis. General acid-base catalysis relies on a protor donor or acceptor other than water. Proteases rely on proton transfer to create strong nucleophiles from active-site amino acid residues. In the protease chymotrypsin, an active-site serine is a potent nucleophile. A nearby residue, His 57, interacts with serine to increase its reactivity. A schematic of chymotrypsin's active site illustrates the active site Ser 195 and His 57 R groups. The Asp 102 residue helps position the His 57 residue via hydrogen bonding. Asp 102 [His] [His+] His 57 6.0 -H-N Chymotrypsin is a digestive enzyme with a catalytic optimum between pH 7.8 and 8.0. However, due to the presence of gastric juice, chymotrypsin often functions in an environment of pH 5.5-7.0. Incorrect The imidazole group of free histidine has a pK₂ of 6.0. Use the…arrow_forwardThe formation of thymidylate is typically coupled with the synthesis of which amino acid? O Cysteine Glutamate Alanine Serine O Glycine O Glutaminearrow_forwardThe highest energy point of the serine protease reaction is the formation of the tetrahedral oxyanion intermediate on the original carbonyl carbon of the scissile peptide bond. True or False? DIPF is an irreversible inhibitor of serine proteases. True or False? The acyl-enzyme intermediate is the transition state of the reaction. True or False? Serine proteases are classified as isomerases. True or False?arrow_forward
- I would appreciate helparrow_forwardWhat does it mean when a person is lactose intolerant? Biologically, what causes this? How can it temporarily be treated?arrow_forwardA mutation has occurred that results in phosphofructokinase not being able to bind ATP in its allosteric site. What impact will this mutation have on the production of ATP in the cell? Select one: a. If no ATP can bind to the allosteric site, then phosphofructokinase will not be able to add the phosphate to fructose-6-phosphate to make fructose-1,6-bisphosphate and glycolysis will not work. So no pyruvate, not cellular respiration. b. If ATP cannot bind to the allosteric site, phosphofructokinase will not be activated to make more ATP by substrate-level phosphorylation. c. No impact on the production but will not be able to effectively shut off over production of ATP with feedback inhibition.arrow_forward
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