lete this portion until 9.22, if so- just submit the first page of this worksheet)Refer to the figure shown. Suppose that three critical amino acids in the active site of a specific enzymeare lysine, histidine, and arginine.HYDROPHOBIC AMINO ACIDSHYDROPHILIC AMINO ACIDS*H,N- CH -CO"H,N-CH- COO H,N-CH-COOPolarWhich of the followingcharacteristics would you predictthe substrate to possess in orderCH,CH"H,N-CH-COOH,N- CH - C0CH,HC CH,CH,CH,CHAlanine(Ala. A)CHValine(Val, V)CHTHNC-NH,Leucine(Leu, L)Asparagine(Asn, N)Glutamine(Gin, Q)to bind the active site of this"H,N- CH -COO "H,N-CH-COO "H,N-CH-COOCH"H,N-CH-COO"H,N-CH-COenzyme?CHCH-CHCH2H C- CH,CHOHOHS-CHA. hydrophilic, with a positivechargeSerineThreonineIsoleucine(le, I)Methianine(Met, M)Phenylalanine(Phe, F)(Ser, S)(Thr, T)Basic"H,N-CH-coO*"H,N-CH-COO"H,N- CH-COO"H,N- CH-- C00 "H,N-CH–COOCHCHCH,CH,CH,B. hydrophilic, but unchargedCHCH,NHNHCH,"H;N CH,H -N-)- NHHistidineH,N- CH,C. relatively hydrophobic.OHTryptophan(Trp, W)Tyrosine(Tyr, Y)Lysine(Lys, K)Arginine(Arg, R)(His. H)D. hydrophilic, with a negativechargeAcidic"H,N- CH – COTH,N-CH – C0SPECIAL AMINO ACIDSCH,CH,"H,N- CH-COHN- CH- CO0 H,N-CH - COOCH,HC CH,CHCHSHGlutamic acidAspartic acid(Asp DProlineGlycine(Gly. G)Cysteine(Cys, C)(Pro, P)(Glu, EIn 1-2 sentences, contrast inhibition by competitive inhibitors and allosteric inhibitors

Enzymes They are a kind of proteins which act as catalyst in biological reaction.

Which of the following characteristics would you predict the substrate to possess in order to bind the active site of this enzyme? A. hydrophilic, with a positive charge -COO B. hydrophilic, but uncharged C. relatively hydrophobic. D. hydrophilic, with a negative charge

Which of the following characteristics would you predict the substrate to possess in order to bind the active site of this enzyme? A. hydrophilic, with a positive charge -COO B. hydrophilic, but uncharged C. relatively hydrophobic. D. hydrophilic, with a negative charge

Human Anatomy & Physiology (11th Edition)

11th Edition

ISBN:9780134580999

Author:Elaine N. Marieb, Katja N. Hoehn

Publisher:Elaine N. Marieb, Katja N. Hoehn

Chapter1: The Human Body: An Orientation

Section: Chapter Questions

Problem 1RQ: The correct sequence of levels forming the structural hierarchy is A. (a) organ, organ system,...

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When measuring reaction velocity as a function of substrate concentration, a researcher usually keeps the concentration of enzyme at a constant level. What would happen if the enzyme concentration were not kept constant? A. Vmax would change, but Km would remain constant. B. Both Vmax and Km would change C. Vmax would remain constant, but Km would change D. Vmax would remain constant, but V would change E. None of the above would necessarily occur
What is true about a competitive inhibitor of an enzyme? You can choose more than one a. it binds the active site b. it binds an allosteric site c. it physically blocks the substrate d. it warps the active site e. it can be overcome with large amounts of substrate
When maltose is broken down into glucose monosaccharides, in an enzymatic reaction, the maltosemolecule is properly called:A. the substrateB. the productC. the catalystD. the enzymeE. the inhibitor
As you change the temperature from a low temperature to a high temperature what happens to the rate of an enzymatic reaction, in general terms? A The reaction rate will steadily increase as the temperature increases. B The reaction rate will steadily decrease as the temperature increases. C The reaction rate will start low, then increase, and then decrease again as the temperature increases. D The reaction rate will not change as the temperature increases.
A certain enzyme catalyzes a reaction that uses the compound shown as a substrate. Would the walls of the active site be likely to contain nonpolar, polar, or charged amino acid side chains? Why?
Which of the following does NOT describe enzyme-catalyzed rate acceleration derived from the binding of substrate to enzyme a. repulsion between like charges b. substrate proximity and orientation c. reduction of entropy (increased order) d. desolvation of the substrate by the enzyme active site e. introduction of strain in bonds that need to break
Can you please solve the following question, both parts please.
You are observing an enzyme driven reaction. To the reaction mixture you add a chemical X which inhibits the reaction. If you add more substrate, the reaction rate approaches the Vmax of the uninhibited reaction. Furthermore, the structure of X is similar to the natural substrate. What kind of inhibitor is X?