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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- BIOCHEMISTRY DRAWING. pls accept question only if 100% confident please and thank you. Enalapril is inactive until acted upon by an esterase. Draw the structure of the resulting bioactive derivative. Hintarrow_forwardSelect all that apply. What is true about the conformational aspects of coupling? O The proton gradient is involved in the release of bound ATP from the synthase as a result of conformational change. O The conformational states interconvert as a result of proton flux through the synthase. There are two sites for substrate on the synthase and two possible conformational states: open (0) and tight-binding (T). Dinitrophenol binds to and inhibits ATP synthase conformational changes, thus inhibiting ATP synthesis. The Fo portion of ATP synthase acts as a rotary motor.arrow_forwardI only need aarrow_forward
- 29. Labels. Suppose that you had an in vitro fatty acid- synthesizing system that had all of the enzymes and cofactors required for fatty acid synthesis except for acetyl CoA. To this system, you added acetyl CoA that contained radioactive hydrogen (³H, tritium) and carbon 14 (¹4C) as shown here. 3H O 14 3H-C-C SCOA 3H The ratio of ³H/¹4C is 3. What would the ³H/14C ratio be after the synthesis of palmitic acid (C₁6) with the use of the radioactive acetyl CoA?arrow_forwardWhy is the reaction rate low at pH7? Be specific and say something about the enzyme structure at the molecular level!arrow_forwardThis has multiple optionsarrow_forward
- Need help, please. Not too sure why my answer is incorrect. Please show all steps/work.arrow_forwardATP. Draw an ATP molecule and have an arrow pointing to the 'high-energy' bonds. See figure 6.13 for help.arrow_forwardprotease mechanism: you isolate a new protease which cleaves the peptide bond 2 aa residues before a F residue. You might expect to fınd... O An I residue in the S2'pocket AL residue in the S2 pocket O aV residue in the oxyanion hole An Lresidue in the catalytic triad in Michaelis-Menton kinetics, cutting the enzyme concentration in half will O will double the reaction rate O will not change Vo and Vmax will change Vo but not turnover number decrease Km by halfarrow_forward
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