8.1 HO.но-ОнO-R27. Since the substrate is a saccharide, what can be inferred about the active site of the enzyme?A. The active site has several hydrogen-bond forming residues.B. There are exposed amino groups in the active site.C. The covalent bonds in the active site are temporary.D. Protein folding is caused by the interaction with the substrate.28. Which of the following statement is TRUE about this transition state?A. The anomeric carbon became a sp2-hybridized carbon.B. Bond lengthening occurred due to nucleophilic attack.C. Hydrogen bonds were formed with the anomeric carbon.D. The anomeric carbon became oxidized efficiently.29. The active site of amylase can also be filled up by maltose, which can be cleaved into glucose molecules. How do youclassify maltose?A. Competitive inhibitorB. SubstrateC. Non-competitive inhibitorD. Allosteric inhibitor

The conformation of an enzyme refers to the specific three-dimensional shape of the protein…

Answered: HO. но- он 27. Since the substrate is a…

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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A. Which enzyme model involves the enzyme staying the same shape when the substrate binds to it? (lock and key, induced fit) B. If an inhibitor has similiar structure to that of a substrate, does it act as a competitive or noncompetitive inhibitor? C. What is the surface for an active site for an ezyme that binds the substrate to that site?
1)Catalase a. Is catalase activity endothermic or exothermic? b. What classification of enzyme is catalase? c. Give the Enzyme Commission (E.C.) number of catalase. d. Is catalase reusable? answer all and don't copy from other sources I will downvote for sure
a. What is the name of metabolite 1? b. What is the name of metabolite 2? c. What kind of reaction occurred when 1 was converted to 2? d. What general kind of enzyme might you expect to perform this reaction? e. What cofactor, if any, would be required for this reaction?
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?
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.)
a. What is the name of metabolite 1? b. What is the name of metabolite 2? c. What molecule a is required for this reaction to proceed? d. What molecule b is produced in addition to 2? e. What enzyme performs this reaction?
nzymes play a fundamental role in cell function. Regarding the biochemistry of enzymes, which of the following statements is correct? A. Most enzymes can bind and react with a wide range of different substrate molecules. B. Enzymes increase the rate of a spontaneous reaction by lowering the ΔG. C. Enzymes increase the enthalpy (H) of the products compared to the reactants. D. Enzymes increase the number of molecules that get to the transition state.
Rearrange the following terms to show the process of enzymatic reaction. Use and + to complete the equation. enzyme enzyme-substrate complex enzyme product substrate Several important things should be noted about this reaction: 1. A/an because of the fit between their structures; 2. As a result, something happens to the example, it might be split in two at a particular location. 3. Then the and 4. The enzyme is again. 5. Note that the arrows in the formula for enzyme reaction point acts on a specific to form a/an molecule. For comes apart, yielding the in the reaction and is now free to react _- This means that the reaction is 6. An enzyme-substrate complex can simply go back to the the 7. The products of an enzymatic reaction can react with the enzyme to form the and again; 8. It, in turn, may again form the 9. Therefore, the same. and the may act to cause a to go either way.
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
Enzymes can be regulated in a many different ways. Covalent modification is one way. Here, the functional groups are attached to or removed from the enzyme. A phosphate group is an example of a functional group that can be added to an enzyme. Depending on the enzyme, addition of a phosphate group can either increase or decrease an enzyme's activity. Evaluate the following names and identify the general name of an enzyme that functions to add phosphate groups to its substrate? A. isomerase B. phosphatase C. kinase D. ligase
The following statements are either True or False. Please label accordingly. a. L-Amino reductase is an enzyme. b. Allosteric enzymes are composed of two or more protein chains. Heavy metals are examples of inhibitors. They function by binding to sulfur on cysteine amino acid residues. C. d. A reversible noncompetitive inhibitor temporarily blocks an enzyme's active site. Enzymes don't denature as easily as smaller proteins when heated or stressed due to their complex secondary and tertiary structure. e. Oxidative phosphorylation is the biochemical process by which ATP is synthesized from ADP when protons cross the inner mitochondrial membrane. f. g. DNA and RNA strands differ only in the fact that DNA forms a double helix. h. There is no secondary structure in RNA strands.
The diagram below shows an outline of the aminotransferase mechanism that skips the specific steps that show how electrons flow when a Schiff base is formed or is hydrolyzed. Using the mechanistic details given below A. Draw the mechanism for Enzyme- PLP Schiff base formation using pyridoxal and the lysine amine group using arrow to indicate electron flow. B.Draw the mechanism for hydrolysis of the Schiff base to form the a-keto acid, which is the reverse of the first reaction.

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