In serine protease catalytic triad mechanism, the first and second products that leaves the active site areCarboxylic acid and amide respectivelyAmide and carboxylic acid respectivelyEster and amide respectivelyCarboxylic acid and ester respectively

Three amino acid residues are involved in the serine protease catalytic triad mechanism. They are…

Answered: In serine protease catalytic triad…

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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Please answer and explain this Biochemsitry Question to the best of your ability
1. Please fully explain (use illustrate where appropriate) the Modes of Enzyme Catalysis exemplified by the serine protease: Chymotrypsin. In your answer discuss employing the illustration whenever possible: the overall reaction mechanism, stability of the reaction transition state, proximity and orientation effects, acid-base catalysis, and covalent catalysis. (c) (0) Ap Asp Toe His Asp 10 C-N bond cleavage HN Ho Ser Ger Binding of substi 196 Ser Gly alto video LBHB NH Sere HAR Proton donation by H (h) Fel of amino product yest OHN Hig Ser Ap (0) Formation of covalent (ES) Alp Me complex Serios
please draw a cysteine - lysine mechanism
Lysozyme’s use of aspartic acid and glutamic acid, to break the glycosidic bonds of the eubacterial cell wall (composed of peptidoglycan), illustrates the common enzymatic pattern of: hydrolysis (catabolic), using nonpolar amino acids at the active site hydrolysis (catabolic), using polar amino acids at the active site condensation (anabolic), using nonpolar amino acids at the active site condensation (anabolic), using polar amino acids at the active site all of the above
give an example like the reaction mechanism of serin protease for example, with pictures & full explanation
Azaserine inhibits amidotransferases. State the purine precursor that resembles azaserine. Which step in the purine biosynthetic pathway will be inhibited?
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
The enzyme which catalyzes the reaction below belongs to which enzyme classification? Н.С— ОН HC=0 C=0 Н-С—ОН H,C-0-P-o- || H,C –0-P-0- O Transfera Hydrolase Isomerase Oxidoreductase
Given the reaction below, what major class of enzyme will catalyze such reaction? Select the correct response: Isomerase Ligase Lyase Transferase Oxido-reductase • Hydrolase
In this step of purine biosynthesis, which functional group gets activated by ATP Pribose NH, ATP Carboxyaminolmidazole ribonedeotide Asp AD Fumarate Pribose NH, S-Aminolmidazole- 4(N-succinylcarboxamide) ribonucleotide O Carboxyaminoimidazole ribonucleotide COOH O Carboxyaminoimidazole ribonucleotide NH2 O Asp side chain COOH O Asp main chain NH2 O Asp main chain COOH
A schematic representation of the enzyme IspD complexed to inhibitor 3, and a series of inhibitors 3-5 are shown below. Ala202 lle240 mwww NH NH Val263 ОН www HN N- lle177 HN 'N' CI 3 X = N 4 X = C-CN 5 X = C-COO IC50 274 µM IC50 140 nM IC50 35 nM NH2 HN Val266 N -N O-H---- N HN %3D Arg157 HN wwww lle265 Explain why structure 4 is a more potent inhibitor (lower IC50 value) than inhibitor 3 and why structure 5 is a much weaker inhibitor (higher IC50 value) than 3 and 4.
What is the mechanism of an enzyme reaction involving a coenzyme for Nucleophilic Addition Rxns? Give

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In serine protease catalytic triad mechanism, the first and second products that leaves the active site are Carboxylic acid and amide respectively Amide and carboxylic acid respectively Ester and amide respectively Carboxylic acid and ester respectively