It is important for a protease to distinguish between two different proteins so that itonly cleaves its target protein. The target protein has the target sequence glu-asp-ser. What amino acids should line the substrate-binding site (the target proteinbinding site) of the enzyme to help it to recognize its target?Amino acids such as glutamate and aspartate.Amino acids such as glutamine and phenylalanine.Amino acids such as arginine and lysine.Amino acids such as tryptophan and cysteine.Any amino acids would work as long as there are three.

The building blocks of proteins are organic substances called amino acids. They have a side chain (R…

Answered: It is important for a protease to…

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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Which of the following amino acids would you expect to find more often near the center of a folded globular protein? Which ones would you expect to find more often exposed to the outside? explain your answers. Ser, Ser-p (a Ser residue that is phosphorylated), Leu, Lys, Gln, His, Phe, Val, Ile, Met, Cys–S–S–Cys (two cysteines that are disulfide- bonded), and Glu. Where would you expect to find the most N-terminal amino acid and the most C-terminal amino acid?
Within an enzyme active site, how does the aspartate carboxyl group activate the histidine nitrogen and convert it into a stronger base?
To answer this question, please reference the Problem Solving Video: pH and pK, of an Amino Acid. Proteases are enzymes that cleave peptide bonds using general acid-base catalysis. General acid-base catalysis relies on a protor donor or acceptor other than water. Proteases rely on proton transfer to create strong nucleophiles from active-site amino acid residues. In the protease chymotrypsin, an active-site serine is a potent nucleophile. A nearby residue, His 57, interacts with serine to increase its reactivity. A schematic of chymotrypsin's active site illustrates the active site Ser 195 and His 57 R groups. The Asp 102 residue helps position the His 57 residue via hydrogen bonding. Asp 102 [His] [His+] His 57 6.0 -H-N Chymotrypsin is a digestive enzyme with a catalytic optimum between pH 7.8 and 8.0. However, due to the presence of gastric juice, chymotrypsin often functions in an environment of pH 5.5-7.0. Incorrect The imidazole group of free histidine has a pK₂ of 6.0. Use the…
What is a major difference between the amino acid biosynthetic capacity of prokaryotic organisms and humans?
Choose any/all amino acids that have a charged/ionized R group at physiological pH. Group of answer choices Arginine (Arg) Asparagine (Asn) Isoleucine (Ile) Valine (Val) Glutamine (Gln) Lysine (Lys)
An animal cell is capable of converting alanine into serine. What is the shortest pathway using known enzymes by which this conversion could be accomplished? Show intermediates and cofactors; no enzyme names are required. (Hint: the first step is the removal of the nitrogen by transamination.)
Consider an amino acid sequence: D1-G2-M3-E4-C5-A5-F7-H8-R9-I10-A11-H12-T13-Y14-G15-F16-P17-E18-A19-A20-M21-C22-K23-W24-E25-A26-Q27-P28 The β-turn structure is likely found at (Write down the residue number). A possible disulfide bond is formed between the residues and . The total number of basic residues are The addition of chymotrypsin will result in blank peptide fragment(s). The addition of trypsin will result in blank peptide fragment(s). The addition of CNBr will result in blank peptide fragment(s).
The highest energy point of the serine protease reaction is the formation of the tetrahedral oxyanion intermediate on the original carbonyl carbon of the scissile peptide bond. True or False? DIPF is an irreversible inhibitor of serine proteases. True or False? The acyl-enzyme intermediate is the transition state of the reaction. True or False? Serine proteases are classified as isomerases. True or False?
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List the name of two amino acids that belong to each of these type of amino acids: Nonpolar (hydrophobic) polar(uncharged) positively charged (basic) negatively charged (acidic)
give an example like the reaction mechanism of serin protease for example, with pictures & full explanation
You are in the process of determining theamino acid sequence of a peptide. After trypsin digestion followedby the Edman degradation, you see the following peptide fragments:

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