Please help with these 4 questions about enzymes and biochemical pathways. Thank you. Answer the following questions about the biochemical pathway shown below.Enzyme 2 Enzyme 3 Enzyme 4→ D EEnzyme 1A-15. What term could you apply to substance A?a. Which terms could you apply to substance B?16. Which enzyme is most likely to have an allosteric site to which the end product E binds?a. What type of enzyme regulation would this be an example of?

Enzymes are biological catalysts present in the body that decrease the activation energy of a…

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Biochemistry

6th Edition

ISBN:9781305577206

Author:Reginald H. Garrett, Charles M. Grisham

Publisher:Reginald H. Garrett, Charles M. Grisham

Chapter20: Electron Transport And Oxidative Phosphorylation

Section: Chapter Questions

Problem 19P

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Explain as brief and simple as possible. Answers must not be more than 30 WORDS each. a. All coenzymes are cofactors, but not all cofactors are coenzymes. Explain this statement. b. How does the induced-fit model of enzyme action explain the broad specificities of some enzymes? c. In competitive inhibition, can both the inhibitor and the substrate bind to an enzyme at the same time? Explain your answer d. Why is penicillin toxic to bacteria but not to higher organisms? e. What is the metabolic basis for the observation that many adults cannot ingest large quantities of milk without developing gastric difficulties?
With appropriate chemical structures, explain the mechanism (mode-of-action) of fluoroacetate poisoning? Example: Step 1: Fluoroacetate is converted to Product “A”. This reaction is catalyzed by Enzyme __________________________ Structures of fluoroacetate and the product “A”. Name of Enzyme. Step 2: Product “A” from Step 1 is converted to Product “B.” Catalyzed by enzyme 2. Structure of Product B and name of Enzyme 2. etc.
The mechanism of chymotrypsin is used as a model for studying enzyme reaction mechanisms. Answer the following questions related to chymotrypsin: 1. List the 3 amino acids in the catalytic triad of chymotrypsin. 2. List the types of catalytic mechanisms (from the 3 main types of catalytic mechanisms) displayed in the mechanism of chymotrypsin.
Suggest the possible class of enzyme (or name of enzyme) for each of theenzyme-catalyzed reactions below. Briefly explain your answer. d. ATP + L-tyrosine + tRNATyr → AMP + PPi + L-Tyrosyl-tRNATyr
Idris has successfully extracted enzymatic proteins from the fish viscera (intestines and stomach). After homogenization and centrifugation, he managed to pool the crude enzyme extract. He is characterizing the enzymes. Please help Idris by answering the followingquestions:(a). How do I determine the enzyme activity? Please give the unit. (b) How do I get the specific activity of this enzyme? Please give the unit.
Select the correct option a.A holoenzyme is a catalytically inactive enzyme in the absence of its cofactor b.An enzyme cofactor is the amino acid side group in the enzyme active site c.Each of the option listed here is true d.An apoenzymes is catalytically active RNA molecule e.A co-substrate is a detachable enzyme cofactor required with another substrate for an enzyme reaction
CHOOSE THE CORRECT LETTER A new metabolic enzyme which utilizes NAD* as a coenzyme. Which of the following could be TRUE based on this information?A. It is involved in an anabolic pathway.B. It performs acetyl group transfer.C. It is involved in a catabolic pathway.D.It catalyzes a hydrolytic cleavage.
Select all FALSE statements about allosteric enzymes. a. They interconvert between a more active form and a less active form. b. They tend to have a hyperbolic curve of ?0 vs. [S]. c.They conform to Michaelis–Menten kinetics. d. They are generally small single subunit proteins. e. They may have binding sites for regulatory molecules that are separate from active sites.
Citrulline is one metabolite whose levels are “out of range.” The unusual levels of citrulline could be explained bythe loss of function of which enzyme? Draw the reaction catalyzed by this enzyme.
(a) Give the substrate for each of the following enzymes: (i) urease (ii) fructose oxidase (b) What is the difference between competitive and noncompetitive inhibition? (c) In feedback control, what type of regulator slows down the catalytic activity of the reaction series? Why aren't intermediate products in a reaction sequence used in feedback control?
a. Provide a name for both metabolites. b. What kind of reaction occurs here? c. What enzyme performs this reaction? d. What cofactors (if any) are involved in this reaction? e. Thermodynamically, this reaction is unfavorable. What allows for this reaction to proceed in the cell? **pls help me with this homework question!!** these questions pertain to the image attached
Which of the following enzymes are required for the shown reaction?a. a-ketoglutarate dehydrogenaseb. dihydrolipoyl dehydrogenasec. Both a and bd. Neither a nor b

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