The active site of an enzyme has the following amino acid residues as critical mediators of catalysis: Ser-134, His-347, Tyr-121 and Glu - 406. What are the most likely specific mechanisms of catalysis by these amino acid residues?

Q: Under the following conditions, fill in the blanks. Then, describe why this inhibitor is the type of…

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Q: The following reaction is catalyzed by this type of enzyme? COO™ COO™ HIC-H HIC-H COO™ succinate…

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Q: Suppose that the active catalytic site of an enzyme contains amino acid residues at the following…

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Q: Which statement is false for transition-state analog enzyme inhibitors? They fit the active site…

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Q: You have discovered a new enzyme that has a nearly identical active site to chymotrypsin. This new…

A: As given peptide is Asn-Phe-lys, and discovered enzyme cleaves at C terminal of non ionizable polar…

Q: , non-ionizable R groups.

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Q: Given the following enzyme-catalyzed reaction, identify the class and subclass of the enzyme…

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Q: What is formed when serine 195 acts as a nucleophile on the carbonyl carbon of the peptide bond?…

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Q: why is biocatalysis over inorganic catalysts in enzyme catalysis favored?

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Q: structural analogues of an enzyme's transition state intermediate act as a competitive inhibitor…

A:

Q: Is the following true or false? Biocatalysis is limited to the use of enzymes found naturally in…

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Q: Snake venom contains many hydrolase enzymes, including several serine proteases. One such protease…

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Q: Propose a plausible enzyme mechanism for triose kinase, the enzyme that catalyzes the conversion of…

A: Triose kinase, like other kinases, catalyses the transfer of phosphate group from ATP to acceptors…

Q: During chymotrypsin-mediated catalysis, which of the following statements is true?  Select any/all…

A:

Q: Certain glutamine analogs irreversibly inactivate enzymes that bind glutamine. Identify the…

A: Nucleotides are ubiquitous as they are involved in majority of biochemical reactions. All of the…

Q: TPCK is a molecule with large hydrophobic groups. Why does TPCK inactivate chymotrypsin but not…

A: Proteases are enzymes responsible for cleaving peptide bonds. Chymotrypsin and trypsin are both…

Q: What does it mean to say that an enzyme- catalyzed reaction is either enzyme limited or substrate…

A: The enzymes are the biocatalyst, which speeds up the chemical reaction in the body. The enzymes do…

Q: Which of the following statements is not true about the catalytic triad in chymotrypsin?  Group of…

A: The objective of the question is to identify the incorrect statement about the catalytic triad in…

Q: All of the following statements about competitive and non-competitive inhibitors are true EXCEPT:(a)…

A: Enzyme Regulation -- Enzyme regulation is done by other molecules which either increases or…

Q: Diisopropylphosphofluoridate (DIPF) inactivates chymotrypsin by covalently modifying serine 195.…

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Q: How would the activity of a reaction catalyzed by a version of subtilisin with all three residues in…

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Q: Draw the catalytic triad of a serine protease at the first tetrahedryl intermediate stage.  Your…

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Q: During glycogen synthesis, glucose-1P is converted into a molecule called UDPG. This reaction also…

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Q: “Caspase” describes the catalytic activity of this enzyme. What amino acyl residue participates in…

A: Caspases are enzymes which mainly take part in programmed cell death. A part from that they also…