. Propose a chemical mechanism for the reaction catalyzed by thePLP-dependent glatamate 1-semialdehyde aminomutase.

Glutamate-1-semialdehyde 2,1-aminomutase is an enzyme which belongs to the family isomerases;…

Answered: . Propose a chemical mechanism for the…

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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Similar questions

Trypsin uses a nearly identical mechanism as chymotrypsin (including the catalytic triad his57-ser195-asp102. beginning with the enzyme substrate complex draw the complete steps in the trypsin mechanism that occur to release the first product and create the acyl enzyme intermediate in the trypsin active site. The substrate for trypsin to be used is gly-lys-gly-ala
Briefly explain how ester hydrolysis experiments helped to provide evidence for the mechanism of peptide hydrolysis catalyzed by chymotrypsin.
Compare and contrast the biological roles of the following amino acids the following pairs ofamino acids. Once you have documented these role state which member of the pair is most important and why.
What are the amino acids of the catalytic triad of chymotrypsin? State the mode of catalysis shown by each of the amino acids that you have named. (a) (b) Predict what will happen if aspartic acid of the triad is replaced by asparagine. (c) Briefly explain the role of the oxyanion hole for the catalysis of chymotrypsin.
Consider the complete oxidation of one mole of simple TAG containing behenic acid residues (22:0). I. For one mole of the fatty acid residue, determine the following: c. What is the number of ATP yield obtained from FADH2 coming from the complete β-oxidation of the fatty acid residue
. The allosterically regulated enzyme ATCase binds aspartic acid as a substrate and acylates the a-amino group. Succinate acts as a competitive inhibitor of ATCase because it binds the active site but can't be acylated. The dependence of vo on [aspartic acid] for ATCase is shown in panel (a) of the accompanying figure. Panel (b) shows the effect of increasing [succinate] on v, when [Asp] is held at a low concentration (see thick vertical arrow in panel (a)). Note that in panel (b), vo is not zero when [succinate] =0 (see thin horizontal arrow). Explain the shape of the curve in panel (b). Why does v, increase initially, before decreasing at higher [succinate]? Co0- COO CH2 CH, HC -NH, CH, COO COO Asp Succinate [Asp) [Succinate] [Asp] in experiment b (a) (b)

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. Propose a chemical mechanism for the reaction catalyzed by the PLP-dependent glatamate 1-semialdehyde aminomutase.