If a serine protease has a moderately deep but very wide hydrophobic pocket within the active site, which substrate amino acid side chains likely are found there during catalysis. List all that apply. Use single letter codes (in capitals) in alphabetical order.
Serine proteases are the enzymes which cleave the peptide bond in proteins by using a serine residue as a nucleophile.
Serine proteases include trypsin, chymotrypsin, and elastase. Chymotrypsin has an active site containing a deep hydrophobic pocket where the substrate amino acids, for example, Phenylalanine, Tyrosine, and Tryptophan binds. Thus the side chain of aromatic amino acids can be found there during catalysis. The single letter codes are F, W, and Y.
If a serine protease has a moderately deep but very wide hydrophobic pocket within the active...
If a serine protease has a moderately deep but very wide hydrophobic pocket within the active site, which substrate amino acid side chains likely are found there during catalysis. List all that apply. Use single letter codes (in capitals) in alphabetical order.
Consider the hypothetical serine protease below, which shows the specificity pockets. The S1 pocket has a glutamic acid in the bottom, the S2 pocket is small and hydrophobic, and the S1\' pocket is deep and hydrophobic. Suggest a 3 amino acid sequence that this protease would cleave and indicate between which sites the peptide bond would be broken.
Cysteine proteases are catalytically homologous to serine proteases, where the active site serine is replaced with a cysteine. What would be the appropriate order of the mechanism? Just write the numbers in order. Peptide bond is cleaved and C becomes sp2 The acyl-enzyme is formed by the transfer of the proton from the positively charged histidine residue, acting as a general acid, to the amino group of the substrate. The side-chain of the amino acid residue immediately before the scissile...
Under typical conditions, many essential biochemical reactions proceed so slowly that life could not exist without the presence of enzymes. Enzymes increase reaction rates through a wide variety of mechanisms. These mechanisms generally utilize the following strategies: improving the nucleophiles and electrophiles present in the catalytic R groups or substrates; stabilizing the extra electron density of the leaving group; and stabilizing transition states. Proteases are enzymes that break down proteins by hydrolyzing peptide bonds. Chymotrypsin is a protease found in...
41. points) a) Draw the catalytic triad as it appears in the active site of any serine protease: b) The following hexapeptide was cut with trypsin. thr-val-glu-lys-his-gin Using the single letter amino acid code, write the sequence of the ping pong reaction in the boxes provided below. Enzyme -Enzyme Double-displacement reaction c) You mutate the S1 pocket of trypsin from Glutamate to Isoleucine. What are the two new products of the digestion of the hexapeptide in part b (still use...
A DNA molecule has many phosphate groups, as shown below What type of amino acid side chains would be most likely be involved in binding this substrate at the active site? Select one polar, negatively charged polar, positively charged hydrophobic polar neutral
33, 48 Depicted below are a peptide substrate and the three catalytic residues within the chymotrypsin active site Note that the 2-dimensional geometry is only roughly shown. R1 represents a large hydrophobic amino acid and R represents other amino acids. The R groups of the catalytic triad of aspartate (Asp102), serine (Ser195), and histidine (His57) are shown. Select the atoms that act as nucleophiles and electrophiles in the acylation phase of the reaction Scroll down for more of this question...
single letter abbreviation of all amino acids that correspond 4. Amino acids. The side chains of amino acids have a wide spectrum of chemical and physical properties. In each sp. provided below, write the single-letter abbreviations of all amino acids that match the description positively charged side chains at pH 7.4 negatively charged side chains at pH 7.4 negatively charged side chains at pH 12 achiral contains two chiral carbons side chain restricts the rotation of main chain contains carboxamide...
biochemistry class homework Under typical conditions, many essential biochemical reactions proceed so slowly that life could not exist without the presence of enzymes. Enzymes increase reaction rates through a variety of mechanisms. These mechanisms generally utilize strategies such as improving the nucleophiles and electrophiles present in the catalytic R groups or substrates, stabilizing the extra electron density of the leaving group, and stabilizing transition states. Proteases are enzymes that break down proteins by hydrolyzing peptide bonds. Chymotrypsin is a protease...
Under typical conditions, many essential biochemical reactions proceed so slowly that life could not existade without the presence of enzymes. Enzymes increase reaction rates through a wide variety of mechanisms These mechanisms generally utilize the folowing strategies: improving the nucleophiles and electrophiles present in the catalytic R groups or substrates; stabilizing the extra electron density of the leaving group; and stabilizing transition states Proteases are enzymes that break down proteins by hydrolyzing peptide bonds. Chymotrypsin is a pryodeoph bic amino...