A carboxypeptidase is a metalloenyme (its active site contains one or more metalions essential for the function) that catalyzes the hydrolysis of the peptide bond of theterminal amino acid of a polypeptide chain (where the free carboxyl group occurs).The binding of an L-alanyl-L-tyrosine peptide substrate in the active site of theenzyme is represented in the scheme below:GluZn++COO™OHH3CCH₂HCNHIO CHHPoche apolaire-HHO+N: C NHHHNH₂Arg 145Туг 248NB: This scheme gives a planar representation of the spatial structure of the activesite where indicated contacts (hatched lines) are supposed to occur in the 3Dstructure of the enzyme.1- Describe the interactions that occur between the ligand and amino acid residuesof the active site.2- What would be the impact on the Km value if we replace L-alanyl-L-tyrosine by thefollowing substrates: L-alanyl-L-phenylalanine; L-alanyl-L-aspartate; L-aspartyl-L-tyrosine.

An active site of an enzyme is a three dimensional structure that occurs within the enzyme. An…

Answered: A carboxypeptidase is a metalloenyme…

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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UDP-glucuronosyltransferase enzymes bind the organic compound UDP-glucuronic acid (UDP-GA) in order to catalyse the transfer of a glucuronic acid group from UDP-GA to a drug molecule, releasing UDP from the active site as a product. UDP is then regenerated by the activity of another enzyme. What terms could be used to describe UDP-GA?
Amino transferases catalyze the transfer of amino groups to alpha-keto acids with pyridoxal phosphate as the prosthetic group. Pyridoxal phosphate can accept an amino group, and its aminated form, pyridoxamine phosphate, can donate its amino group to an alpha-keto acid. Draw the detailed mechanism of the transamination reaction in the active site of an aminotransferase. Use the glutamate oxaloacetate transaminase as an example.
the following is a coenzyme or cofactor involved in enzymatic reaction. identify the biochemical role that S-adenosylmethionine plays within a biochemical tranformation.
The enzyme chymotrypsin, catalyses the hydrolysis of nitrophenyl acetate and pther acyl esters. Name the amino acid residue, the side chain of the residue, and the type of bond/linkage involved in the formation of the acyl-emzyme complex during catalysis.
Amino transferases catalyze the transfer of amino groups to alpha-keto acids with pyridoxal phosphate as the prosthetic group. Pyridoxal phosphate can accept an amino group, and its aminated form, pyridoxamine phosphate, can donate its amino group to an alpha-keto acid. Illustrate the detailed mechanism of the transamination reaction in the active site of an aminotransferase. Use the glutamate oxaloacetate transaminase as an example.
Show the complete reaction mechanism for the deamination of alanine until the amino group is transferred to the keto acid acceptor ⍺-ketoglutarate
Beginning with the 1st tetrahedral intermediate, show the complete steps in chymotrypsin mechanism that occurs to form the 2nd chymotrypsin intermediate in the chymotrypsin active site. The substrate for chymotrypsin to be used is Ala-Tyr-Gly. Further, name the amino acid(s) that would be released as a result of the reactions you'd illustrated above.
Lysozyme is an antibacterial enzyme found in animals. Residues Asp 101 and Arg 114 are required for efficient catalysis, although they are located at some distance from the active site Glu 35 and Asp 52. Substituting Ala for either Asp 101 or Arg 114 does not significantly alter the enzyme's tertiary structure, but significantly reduces its catalytic activity. Explain.
Several names are compatible with standard nomenclature for the enzyme that catalyzes the reaction shown in the figure. However, the assigned name is based specifically based on its substrate and its coenzyme. What is that name?
Fatty acids are converted to their coenzyme A esters in a reversible reaction catalyzed by acyl-CoA synthetase: R-COO +ATP +COA R-C-COA +AMP + PPi a) The reaction involves two steps the first of which forms an enzyme-bound intermediate identified as the mixed anhydride of the fatty acid and AMP: R-C-O-P-O-nibose-adenine Write two chemical equations coresponding to the two steps of the reaction catalyzed by the synthetase. b) The acyl-CoA synthetase reaction as written above is readily reversible. How might the reaction be made to favor formation of fatty acyl-CoA? Write within the box. Anything outside the box will not be graded. From the
the structures of chymotrypsin and other serine proteases revealed that the active sites of these enzymes shared a particular sterochemical arrangement of residues crucial to their activity. This came to be known as the catalytic triad, as it consisted of the oponyomous serine (Ser) residue, along with a histidine (His) and an aspartate (Asp) residue. Which of the following would result in the greatest decrease in function of the catalytic triad found in serine proteases? O Mutation to Ser, Cys, Asp O Mutation to Ser, His, Asp O Mutation to Cys, His, Asp O Mutation to Ser, His, Glu
Lysine degradation requires removal of two amino groups. Removal of itsε-amino group gives a-aminoadipic semialdehyde. This product is thendegraded to acetoacetate by the same chemical strategy used to degrade thebranched-chain amino acids. Draw the proposed intermediates in this pathway (Hint: see Figure 18.14).

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