The mechanism of chymotrypsin can be viewed as a two-step process, acylation of the enzyme active site followed by adeacylation reaction.What accounts for the observed "burst" in rapid kinetic studies of the hydrolysis of N-acetyl-L-phenylalanine p-nitrophenylester by chymotrypsin?The rate of hydrolysis of the acyl-enzyme intermediate is faster than the rate of forming the acyl-enzyme intermediate.The rates of the acylation and deacylation reactions are equal.The rate of the acylation reaction is slower than the rate of the deacylation reaction.The rate of the acylation reaction is faster than the rate of the deacylation reaction.

A burst in rapid kinetic studies (i.e. pre-steady state studies) is a high rate of product release…

Answered: The mechanism of chymotrypsin can be…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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Malate dehydrogenase has a ΔGo′ΔGo′= 29.5 kJ/mol for the formation of oxaloacetate from malate yet plays a crucial role in the Citric Acid Cycle. Explain (briefly) how this enzyme with a very non-spontaneous ΔGo′ΔGo′can function well in a biochemical pathway.
make a schematic diagram of BChE/AChE inhibitory determination Butyrylthiocholine iodide (BChI), as well as acetylthiocholine iodide(AChI) molecules were utilized as substrate compounds of the reaction. Inthis regard, 5,5′‐dithio‐bis(2‐nitro‐benzoic acid) compound (DTNB) wasused to estimate BChE/AChE activity. In summary, 100 μL Tris buffersolution (HCl, 1.0M, pH 8.0, Tris) and variety of concentrations of thesample solution (50‐200 mL) were added in deionized water and also20 μL of BChE/AChE enzymes solutions added. The mixture was thenincubated for 10 minutes at 20°C. Finally, 50 μL of DTNB (0.5 mM and25 mL) BChI/AChI were added to the incubator mixture. The reactionwas also started by adding 50 μL BChI/AChI. The activity of theseenzymes was evaluated using spectrophotometric spectra with awavelength of 412 nm.
In 1937, two German biochemists published a paper proposing these reactions as part of glucose oxidation: citrate → isocitrate → α-ketoglutarate →succinate → fumarate → malate → oxaloacetate. Adding succinate, fumarate, or malate to thin slices of tissue increased oxygen consumption, supporting the hypothesis that these molecules are intermediates in the process. However, they were puzzled by the observation that these intermediates were still present in the reaction mixture at the end of the experiment. They had thought that intermediates would be consumed as they were converted to the next molecule in the pathway. What explains the observation that these intermediates were still present? a) The pathway is a cycle, constantly regenerating intermediates as glucose is broken down. b) Succinate, fumarate, and malate are not reactants but catalysts, and catalysts are not consumed in the process. c) Succinate, fumarate, and malate increase metabolism and therefore oxygen consumption,…
Isocitrate labeled with 14C at positions 2 and 5 was isolated from cultured liver cells administered [methyl-14C pyruvate] and enough malonate to completely inhibit succinate dehydrogenase. Explain how this can happen.
Draw the Catabolism of triacylglycerols- beta-oxidation pathway, then identify and label the different types of organic reaction mechanisms (Sn1, Sn2, E1, or E2 reaction mechanisms). Make sure to name and draw the structures of each biomolecule included in the pathway.
Suppose a liver extract capable of carrying out normal metabolic reactions (including gluconeogenesis) is incubated with pyruvate partially labeled with deuterium at the methyl group (see below: D= deuterium, i.e., H-2) a) Explain why the oxaloacetate formed in step 1 of gluconeogenesis is only partially labeled (i.e., some of the oxaloacetate is labeled and some is not). b) Where would the label be found in glucose?
Given the following statements, identify which are true and which are not. (1) Two ribose subunits are present in the coenzyme flavin adenine dinucleotide. (2) In the common metabolic pathway, 10 molecules of ATP are produced per acetyl CoA catabolized. (3) The purpose of step 2 in the CAC is to convert a secondary alcohol to a tertiary alcohol.
Which of the following biochemical conversions can be carried out by the least number of proteins? Assume proper metabolic conditions, abundance of cofactors, necessary accessory molecules, etc. 1 propionyl-CoA → 1 succinyl-CoA 1 palmitate (16:0) → 8 acetyl-CoA 1 acetyl-CoA + 7 malonyl-CoA → 1 palmitate (16:0) 1 palmitate (16:0) → 1 acetyl-CoA + 1 myristic acid (14:0) 1 acetyl-CoA → 1 succinate Please answer very soon will give rating surely
When the identical subunits of chicken liver fatty acid synthase are dissociated in vitro, all of the activities can be detected in the separated subunits except for the β-ketoacyl synthase reaction and the overall synthesis of palmitate. Explain these observations.
Diazepam is converted in vivo to an active metabolite Oxazepam. Explain metabolic transfomation of diazepam to oxazepam. (Provide names of enzymes involved in this transformation. Drawings of structures ofintemediate metabolites is NOT required)

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