Covalent enzyme catalysis involves the formation of a transient covalent bönd between an enzyme and its substrate. Below is the general structure of a commonly encountered so-called acyl-en En NH O-C-R OH En- Select amino acid residues from the table beiow that have side chains with the enzyme reactive groups indicated in the above reaction (if more than one, start with lowest numbered first). Amino acid No 3-letter code What is the chemical name of the acyl-enzyme intermediate compound (acylimidazole, anhydride, ester, Schif base, thioester)?

Covalent enzyme catalysis involves the formation of a transient covalent bönd between an enzyme and its substrate. Below is the general structure of a commonly encountered so-called acyl-en En NH O-C-R OH En- Select amino acid residues from the table beiow that have side chains with the enzyme reactive groups indicated in the above reaction (if more than one, start with lowest numbered first). Amino acid No 3-letter code What is the chemical name of the acyl-enzyme intermediate compound (acylimidazole, anhydride, ester, Schif base, thioester)?

Introduction to General, Organic and Biochemistry

11th Edition

ISBN:9781285869759

Author:Frederick A. Bettelheim, William H. Brown, Mary K. Campbell, Shawn O. Farrell, Omar Torres

Publisher:Frederick A. Bettelheim, William H. Brown, Mary K. Campbell, Shawn O. Farrell, Omar Torres

Chapter22: Proteins

Section: Chapter Questions

Problem 22.99P

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) The correct name of the is: NH2 CH XOL NO₂ SO3H gc) 2-amino-3-methyl-5-nitro benzenesufonic acid ut) 1-amino-3-methyl-4-nitro-6-benzenesufonic acid ro) 6-amino-4-methi-3-nitrobenzenesufonic acid tb) 2-amino-4-methyl-5-nitrobenzenes ufonic acid
please explain why this happends, im having trouble in this section. Part A Chymotrypsin, an enzyme that hydrolyzes peptide bonds in proteins, functions in the small intestine at an optimum pH of 7.7 to 8.0. How is the rate of the chymotrypsin-catalyzed reaction affected by each of the following conditions?
All amino acids have two ionizable functional groups: an a-amino group (average pK, of 9.4) and an a-carboxylic acid group (average pK, of 2.2). Tyrosine also has an ionizable side chain (R group) with a pK, of about 10.1. One of the possible ionization states of tyrosine is shown. H3N-CH -C-OH CH2 ÓH At what pH would the structure be the predominant ionization state? Consider the ionization state of all three of the functional groups. The protonated form of the R group of tyrosine is shown in the structure. The ratio of the protonated form to the charged (deprotonated) form depends on the pK, of the R group and the pH of the solution. Select the pH value at which the charged form of the R group would predominate.
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During acidosis of a protein, shown below, salt bridges are broken, resulting in denaturation. Which choice shows the products of alkalosis?
provide brief explanation thnks
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