Human Anatomy & Physiology (11th Edition)
11th Edition
ISBN: 9780134580999
Author: Elaine N. Marieb, Katja N. Hoehn
Publisher: PEARSON
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Researchers thought that by comparing the shapes of the active sites of chymotrypsin and subtilisin, they would be able to learn more about the molecular structure of both enzymes. However, this did not happen. I'm interested in what you think about how well this strategy works.
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- C)|Myth: The specificity of an enzyme for its substrate is explained by the lock and key hypothesis. Fact: The lock and key hypothesis is outdated! What is our current model for understanding regarding how enzymes recognize and bind to substrates?arrow_forwardWhich of the following is true about allosteric enzymes? A. Allosteric enzymes are always multimeric. B. Regulatory sites (allosteric sites) on an allosteric enzyme are always different from the catalytic site. C. Allosteric enzymes always change the conformation of the active site in response to binding of an allosteric modulator. D. Suicide inactivators are examples of allosteric modulators.arrow_forwardA dichotomous key works by determining positive and negative reactions to different biochemicals. Why does this method allow us to identify one species of organism from another? – for this question, do not describe the dichotomous key procedure, think about why it works, what are biochemical reactions based on? Think enzymatic pathways, what are enzymes, what are they a reflection of? Keep the answer between 2-3 sentencesarrow_forward
- A) Myth: Enzymes are specific for one substrate. Fact: Like most enzymes, alliinase can act on multiple different substrates. Explain why most enzymes can act on more than one substrate compound. (Refer to the “Alliin-like Substrates" panel in your answer.)arrow_forwardCan you help me, please? Enzyme inhibition (compare and contrast reversible and irreversible inhibitors)arrow_forwardUsing the Acronym LILHOT, give the 6 major families of enzymes found in biological systemsarrow_forward
- Watch this video and answer the question below https://youtu.be/AtlCxYDxY1I BCR-ABL is a kinase. A kinase is a type of enzyme that catalyzes the transfer of phosphate from one molecule to another. What are the substrates for the reaction that BCR-ABL catalyzes? Select all that are true.a- Substrate protein b- BCR-ABL c-ATP d- None of the listed molecules herearrow_forwardProteases are one of the main drug targets. Choose the False statement regarding proteases. A. Proteases are enzymes that cleave peptide bonds. B. Water is a reactant in the reaction catalyzed by proteases. C. Proteases, like all enzymes show substrate specificity, meaning they cleave only substate that fit the bonding product. D. Proteases rely on the proton transfer from NADH to the substrate. E. Protease mechanism involves only acid-base catalysis.arrow_forwardExplain why it is normal for two enzymes that have vastly different amino acid sequences, still be able to catalyze similar enzymatic reactions.arrow_forward
- The cytochrome P450 family of monooxygenase enzymes are involved in the clearance of drugs/medications from our body. Many adverse drug -drug interactions are known to occur as a result of interaction with the cytochrome P450 enzymes. A large number of drugs are metabolized by the enzyme P450 3A4. Human P450 3A4 is known to metabolize midazolam, a sedative, to a hydroxylated product, 1'- hydroxymidazolam. The kinetic data shown below are for the reaction catalyzed by P450 3A4. a. Focusing on the first 2 columns, determine the Km and Vmax for the P450 3A4 enzyme. b. Ketoconazole, an antifungal drug, is known to cause adverse drug interactions when taken along with midazolam. Using the data in the table, determine the type of inhibition caused by ketoconazole. Explain how you arrived at your answer. Midazolam (uM) 00 AN1 2 14 8 Rate of product formation (pmol min-1) 100 156 222 323 Rate of product formation in presence of ketoconazole pmol min-1) 11 18 27 40arrow_forwardScientists uncover a new pathway for synthesis of Threonine (see below). They also identify mutants that cannot grow on media lacking threonine (Thr-1, 2 and 3). These mutants have mutations in separate enzymes in this pathway. They are able to grow when different supplements are added to the media (see below). Based on this, what is the order of the enzymes in this pathway? a. Thr-2, 1, 3 b. Thr-2, 3, 1 c. Thr-1, 2, 3 d. Thr-3, 2, 1arrow_forward
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