Which of the following statement is CORRECT?O Hydrolysis of starch into glucose in an elimination reactionGroup transfer reaction is a nucleophilic substitution reactionConversion of 3-phosphoglycerate to 2-phosphoglycerate is a group transfer reactionMost biochemical reaction occurs via homolytic cleavageElectrophiles are electron-rich, while nucleophiles are electron-deficient

Biochemical transformations can be classified into different reaction types. Processes like…

Answered: Which of the following statement is…

Biochemistry

6th Edition

ISBN:9781305577206

Author:Reginald H. Garrett, Charles M. Grisham

Publisher:Reginald H. Garrett, Charles M. Grisham

Chapter23: Fatty Acid Catabolism

Section: Chapter Questions

Problem 21P: Using the ActiveModel for enoyl-CoA dehydratase, give an example of a case in which conserved...

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The following reaction is catalyzed by this type of enzyme? Coo COO™ I HIC-H H-C-H COO™ succinate isomerase hydrolase O ligase transferase oxidoreductase succinate dehydrogenase FAD FADH2 H-C || C-H COO fumarate
Consider the mechanism of enolase, as indicated below. Which of the following correctly describes the roles of the Mg2+ as illustrated in the figure? (This is a multi- select question). Mg2+ Mg2 Enolase PO3- OH -C-C-H H OH HO H-N-H Lys 345 Glu211 2-Phosphoglycerate bound to enzyme Mg2+ Mg2 PO3- OH C-C-H OH HO H H-N*-H Lys 345 O Glu211 Enolic intermediate HOH PO3- H Phosphoenolpyruvate The metal ion (Mg2+) is helping to stabilize the extra negative charge that developed on the carboxyl group in the enolic intermediate. The metal ion (Mg2+) is serving as a general base, removing a proton in order to improve the quality of the nucleophile. The metal ion (Mg2+) is assisting in the oxidation of the carboxyl carbon through metal ion catalysis. The metal ion (Mg2+) is helping to orient the substrate properly in the active site. The metal ion (Mg2+) is accepting a proton in order to improve the quality of the leaving group.
Transamination reactions typically involve which of the following (select all that apply)? O almidine linkage/Schiff base O biotin O alpha-keto acid O pyridoxal phosphate zymogens O glutamate dehydrogenase
There is a cysteine protease, which uses a similar chemical mechanism to chymotrypsin except for using cysteine instead of serine during catalysis. Please draw the stepwise chemical mechanism for the cysteine protease.
Catalase speeds the breakdown of hydrogen peroxide in nearly all organisms. True or false?
The reaction catalyzed by phosphorylase is readily reversible in vitro. At pH 6.8, the equilibrium ratio of orthophosphate to glucose 1-phosphate is 3.6. The value of ΔG°’ for this reaction is small because a glycosidic bond is replaced by a phosphoryl ester bond that has a nearly equal transfer potential. However, phosphorolysis proceeds far in the direction of glycogen breakdown in vivo. Suggest one means by which the reaction can be made irreversible in vivo.
A(n) _________ reaction converts glycylalanine to glycine and alanine. This reaction requires __________. Blank 1 options- Oxidation-reduction Hydrolysis Isomerization Group transfer Internal rearrangement Blank 2 options- H2O and apeptidase or a protease H2O and a phosphatase ADP and a phosphatase NAD+ and a peptidase or a protease
Which of the following statements regarding the catalytic mechanism of superoxide dismutase is true? The D residue does not participate in acid-base catalysis during the course of the catalyzed reaction All of the answers are true The coordinated Zn2+ participates in stabilizing Cu²+ in the reduction-oxidation reactions to consume O₂ The Cu²+ coenzyme is coordinated by H residues, positioning it precisely for consumption of 0₂ The overall reaction consumes two equivalents of O₂ and two proton equivalents in order to produces one equivalent H₂O2
The oxyanion hole deprotonates an incoming water molecule to convert it to a potent nucleophile. True or False? The oxyanion hole is comprised of hydrogen bonding atoms that project into a space on the active site that will have all H-bonding potential satisfied only during the catalytic cycle of the reaction. True or False? The catalytic triad residues are all next to each other in the primary sequence of trypsin. True or False?
His388 Glu357 His388 Glu357 Ring opening Proton HO HO abstraction HO но- G6P He NH- NH His388 His388 His388 Glu357 Glu357 Glu357 HO но HO но- но OH cis-enediol F6P Ring closure intermediate OH Describe the mechanism shown above for phosphoglucose isomerase. Describe the chemistry of each step • How the enzyme appears or might facilitate the chemistry How the enzyme increases the reaction rate.
Which of the following statements is true about the chymotrypsin reaction? 1. The catalytic triad at the active site is formed by three residues: His, Gly, and Ser 2. When the substrate is p-Nitrophenylacetate, the rate-limiting step is the release of p-Nitrophenolate. 3. During the reaction, LBHB forms when the proton is donated to His from Ser or water. 4. The chymotrypsin reaction involves “only” specific acid-base catalysis 5. The “oxyanion hole” is formed by the amide nitrogens of Ser and Glu
Which of the following is incorrect about the chymotrypsin mechanism? a. The (-) charge of oxygen in the transition state is stabilized by the oxyanion hole Ob. Asp does not act as a nucleophile Oc. After H₂O had a proton removed, the OH acts as a nucleophile Od. When His removes a proton from H₂O, it is acting as an acid

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