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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Enzymes are stereochemically specific; that is, they often
convert only one stereoisomeric form of substrate into
product. Why is such specificity inherent in their
structure?
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- Distinguish between the concerted and sequential models for the behavior of allosteric enzymes. Give 2 differencesarrow_forwardPlease, please I do not understand this question for Biochemistry. Can you help me? Steps leading to the correct answer would be helpful!arrow_forwardStreptokinase is an enzyme produced by Streptococci bacteria and is used to digest fibrin clots. It is therefore very effective at eliminating blood clots that cause heart attacks and strokes. Why does a physician not worry that injecting streptokinase will also destroy healthy tissue in their patients? – this answer should discuss the specificity of enzymes for their substrates, defined by the shape of the active site.arrow_forward
- Consider the metabolic pathway show below that converts substrate A to B with the enzyme A-ase, B to C with B-ase(I), and so forth. Acety/A-ase Acetate - A-ase Deacetylase A-ase Protease & C-ase B-ase ABCD What is the mechanism of regulation of B-ase? Positive allostery Reversible Covalent modification Isoenzymes Proteolytic Activation Feedback Inhibition 1arrow_forwardWhat role do low-barrier hydrogen bonds play in serine protease catalysis?arrow_forwardThe purified OXA-M290 enzyme can now be tested to determine which β-lactamase inhibitor is most effective. This inhibitor could be prescribed in combination with a β-lactam antibiotic to treat the infection caused by the E. coli KGH1 strain. Before testing inhibitors against OXA-M290, the kinetic activity of this enzyme must first be measured. The activity of OXA-M290 is measured using nitrocefin, a chromogenic β-lactam antibiotic. When nitrocefin is hydrolyzed by a β-lactamase, it changes from yellow to red in colour. The nitrocefin hydrolysis product has an extinction coefficient of 20,500 M-1 cm-1 at 486 nm. The hydrolysis of 60 μM nitrocefin by 1 nM OXA-M290 is monitored using a microplate reader. The absorbance of the wells in the plate is measured at 486 nm every 30 seconds. This experiment is carried out with three replicates, generating the following data: Time (min) Absorbance of Replicate 1 Absorbance of Replicate 2 Absorbance of Replicate 3 0.5 0.0984…arrow_forward
- A Leu side chain can form Schiff base with the substrate during covalent catalysis. True Falsearrow_forwardEnzymatic activity is rapidly destroyed at physiologically high temperatures. How do you reconcile this observation with the existence of bacteria and algae that grow in hot springs where the temperature may be as high as 73 °C?arrow_forwardIn a uni uni enzyme reaction, what is the substrate concentration relative to Km when anenzyme operates at 0.95 * V. What about 0.99 * V?arrow_forward
- The natural enzyme is recreated by mixing isolated regulatory and catalytic subunits of ATCase. What biological relevance does this observation have?arrow_forwardIs the following statement correct or incorrect? It is only possible to employ enzymes that are present naturally in yeast or bacteria for biocatalysis.arrow_forwardFind an enzyme that is used by humans for some industrial or useful process (apart from its original purpose; e.g. food production, textiles, agriculture, clinical diagnosis, medical treatment, biofuel production, material polymerization, etc.). How do we obtain or harvest the enzyme? What reaction(s) does it catalyze, and how is this useful for its industrial purpose? 200 words onlyarrow_forward
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