Biochemistry
9th Edition
ISBN: 9781319114671
Author: Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher: W. H. Freeman
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- The graph displays the activities of wild-type and several mutated forms of subtilisin on a logarithmic scale. 5 The mutations are identified as: • The first letter is the one-letter abbreviation for the amino acid being altered. • The number identifies the position of the residue in the primary structure. The second letter is the one-letter abbreviation for the amino acid replacing the original one. • Uncat. refers to the estimated rate for the uncatalyzed reaction. Log ₁0k cat (S-¹) -5 -10 Wild type D32A S221A H64A İnti. S221A H64A D32A Uncat. How would the activity of a reaction catalyzed by a version of subtilisin with all three residues in the catalytic triad mutated compare to the activity of the uncatalyzed reaction? O It would have more activity, because the reaction catalyzed by the triple mutant is approximately 1000-fold faster than the uncatalyzed reaction. It would have more activity, because the reaction catalyzed by the triple mutant is approximately three-fold faster…arrow_forwardTrue/Faise Question: Enzymes are usually stereoselective for their substrates (can preferentially bind and act only on a D- or an L-isomer of the substrate). O True O ralsearrow_forwardI once got non specific and another time i got uncompetitive and anothe time i got transition state analog please put the right answerarrow_forward
- Draw me the inhibition reaction mechanism of Cysteine Protease Inhibitor (E64). How the epoxide ring is opening because of the reaction with the thiol group of cysteine and what product are being made. Please draw with arrow pushing and also explain the reason of each attack.arrow_forwardIn the following example an enzyme is being inhibited. This is an example of Active site Inhibitor Altered active site O Non-competitive inhibition O Competitive inhibition MacBook Airarrow_forwardEnzymes are stereochemically specific; that is, they oftenconvert only one stereoisomeric form of substrate intoproduct. Why is such specificity inherent in theirstructure?arrow_forward
- PMSF is a protease inhibitor that binds to enzyme active site. What is the possible mode of inhibition? Competitive O Irreversible O Non-competitive O Mixedarrow_forwardA catalase is an antioxidant enzyme that requires ferric ion for catalysis. Under conditions of iron deficiency, when the catalase lacks ferric ion, it would be referred to as: O prosthetic group O holoenzyme ароenzyme coenzymearrow_forwardWhich of the following aspects of catalysis by enzymes can NOT be explained by the Fischer Lock and Key Hypothesis? Enzymes will lower the activation energy barrier for reaction. Enzymes will specifically recognize their substrates. Appropriate substrates will bind to the enzyme to form a Michaelis complex. Enzymes have an "active site" where appropriate substrates will be bound. Two of the above cannot be explained by the Fischer "Lock and Key" Hypothesis.arrow_forward
- What are the effects of different light colors in photosynthesis? Different light colors will change the rate of photosynthesis Light color does not affect photosynthesis Carbohydrates are metabolized by light Photosynthesis does not require lightarrow_forwardTo 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…arrow_forwardplease focus on this question 3 times i submitted it and three different answers, please make sure of ur answerarrow_forward
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