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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Question
- The place on the enzyme where the substrate binds is called the: a) coenzyme b) transition state c) active site d) enzyme-substrate complex
- The enzyme-bound substrate is also called: a) coenzyme b) transition state c) active site d) enzyme-substrate complex
- The enzyme-bound substrate facilitates the formation of the: a) coenzyme b) transition state c) active site d) enzyme-substrate complex
- The binding of substrates to most enzymes may be best described as: a) lock and key b) induced fit c) backside attachment d) cofactor displacement
Expert Solution
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Step 1: Explaining about enzyme
An enzyme is usually made up of protein with different amino acids linked together by peptide bonds. It has a certain specific site which is called active site. Enzyme binds to the specific substrate to convert it into product without itself being used up in the reaction. It increases the rate of reaction by decreasing the activation energy of the reaction.
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- Penicillin and related drugs inhibit the enzyme _____; this enzyme is produced by _____. A) β-lacamase; bacteria B) lysozyme; human cells C) aldolase; bacteria D) transpeptidase; bacteria E) transpeptidase; human cellsarrow_forwardIn what way(s) are Trypsin, Chymotrypsin, and Elastase different? (choose 1) a) They target different amino acid residues in proteins. b) They use different reaction mechanisms c) Both of the above d) Neither of the abovearrow_forwarda) What is the Steady State assumption; how does steady state differ from equilibrium? b) Transition state; what are two ways that enzymes can decrease the transition state energy?arrow_forward
- Can you help mearrow_forwardWhat does an enzyme change relative to an uncatalyzed reaction? a) The rate of the reaction. b) The free energy change of the reaction. c) The size of the active site. d) The pH. e) The equilibrium constant.arrow_forwardA) what are the 6 types of enzymes B) provide real world examples of protein denaturation and explain what is happening during the process C) describe factors that can affect enzyme activityarrow_forward
- 1) Answer the following questions about a Vegetarian diet: a) List Pros and Cons of being on the diet. b) List any possible misconceptions that may have been verified or nullified by scientific articles for this diet. c) What biochemical pathway would this diet target?arrow_forward2. Enzymes A) have highest affinity for the substrate B) have highest affinity for the product C) have highest affinity for the transition state D) None of the above Briefly explain:arrow_forwardWhich is true of reducing disaccharidess: a) One sugar has an unlinked anomeric carbon b) the anomeric carbons of both sugars are linked c) both sugars are ketoses d) one sugar is a ketose and the other is an aldose Amylose differs from amylopectin in that amylose is: a) branched b) unbranched c) required in the diet d) found only in bacteria The structure of glycogen most closely resembles that of: a) cellulose b) amylose c) amylopectin d) egg albumin The structure of cellulose differs from that of amylose in which way? A) cellulose uses fructose while amylose uses glucose b) cellulose has branches while amylose does not c) amylose has branches while cellulose does not d) cellulose has beta-links while amylose has alpha links The following sugar is commonly found in nature: a) L – fucose b) L-glucose c) L-ribose d) L – galactose Hyaluronic acid is classified as a: a) peptidoglycan b) ketohexose c) glycosaminoglycan d)…arrow_forward
- What is the allosteric effect on O2 binding to the second subunit of hemoglobin after the first subunit binds after O2 binding? to 02? What state would hemoglobin be O A decrease in affinity of hemoglobin for 02: T-State O An increase in affinity of hemoglobin for O2: T-State An increase in affinity of hemoglobin for 02; R-State O A decrease in affinity of hemoglobin for O2; R-Statearrow_forwardEnzymes work by... OA) Altering the equilibrium position of a reaction B) Altering the DG value for a reaction C) Increasing the activation energy for a reaction D) Preventing degradation of the product E) Promoting the formation of the transition statearrow_forwardIn competitive inhibition A) a molecule competes for the allosteric site on an enzyme B) two proteins combine C) a molecule completes for the active site on an enzyme D) activation energy is reducedarrow_forward
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