p4 P2 P5' -NH2 OH H H H H H он P5 P3 P2'

Q: How would chymotrypsin's catalytic triad be affected by extremely low and extremely high pH values…

A: Enzymes are catalysts that increase the rate of the chemical reaction without undergoing any change…

Q: If a small amount of ATP labeled with radioactive phosphorus in the terminal position, [γ-32P]ATP,…

A: ATP is made up of adenosine bound to three phosphate groups. Adenosine is made up of adenine and…

Q: The S3’ pocket on PfSUB1 (attached) contains the side chains of Lys465 and Tyr427. Researchers…

A: According to Michaelis-Menten Kinetics, when the rate or velocity of an enzyme catalyzed reaction…

Q: An active site of a hypothetical serine protease with a peptide substrate bound is shown below:…

A: Serine peptidases are enzymes that are mainly concerned with the cleaving of the peptide bonds in…

Q: Lysozyme    is    an    enzyme    that    hydrolyzes    bacterial    cell    wall…

A: Lysozymes are antibacterial agents that have the ability to hydrolyze the cell wall of bacteria. The…

Q: Consider the role of Histidine in the Serine protease mechanism and sketch a plot showing he…

A: Enzymes are biological catalysts that increase rate of biochemical reactions.Serine proteases are…

Q: The mechanism for lysozyme cleavage of its polysaccharide substrate requires Glu35 in its nonionized…

A: The lysozyme is an enzyme found in the secretions like tears and sweat. It cleaves the glycosidic…

Q: Phosphoglycerate kinase shows induced fit resulting from the binding of both substrates to form the…

A: Phosphoglycerate kinase is a glycolysis enzyme that catalyses the seventh reaction in the ten-step…

Q: Match the specificity pocket (identified by red number) to the residue that occupies it. 1 3 4 2 1.…

A: Proteases preferentially hydrolyze polypeptide substrate peptide bonds based on the amino acids…

Q: Lysozyme    is    an    enzyme    that    hydrolyzes    bacterial    cell    wall…

A: Lysozymes are antibacterial agents that have the ability to hydrolyze the cell wall of bacteria. The…

Q: Serine Proteases, such as chymotrypsin, contain Ser/Asp/His as a catalytic triad (i.e. three…

A: The active site of enzymes are among the conserved regions of proteins. If evolution finds an active…

Q: The active site of lysozyme contains two amino acid residues essential for catalysis: Glu35 and…

A: Lysozyme is an antibacterial enzyme that plays a crucial role in prevention of bacterial infections.…

Q: What is the smallest number of molecules of ATP and GTP consumed in the synthesis of a 200- residue…

A: ATP is adenosine triphosphate and is an organic compound. It is a hydrotrope that provides energy to…

Q: The active site of an enzyme that uses a general acid-base catalytic mechanism contains a Glu and an…

A: In simple terms, pH indicates whether a substance is acid or base. pKa determine how strong is an…

Q: The allosterically regulated enzyme ATCase binds aspartic acid as a substrate and acylates the…

A: Aspartate carbamoyltransferase(ATCase) is an enzyme that converts aspartate and carbamoyl phosphate…

Q: Lysozyme is an antibacterial enzyme found in animals.  Residues Asp 101 and Arg 114  are required…

A: Introduction- Lysozyme helps in catalyzation of binding energy where it catalysis the peptidoglycan…

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

A: Diisopropylphosphofluoridate (DIPF) is an irreversible inhibitor of chymotrypsin. It forms a…

Q: Substrate A has a Km of 45uM and a kcat of 100/s with trypsin and a Km of 540mM and a kcat of 2/s…

A: Enzymes are the proteinous structure that helps in increasing the rate of metabolism. The function…

Q: You have isolated a new protease that cleaves peptide bonds on the carboxyl side of Asp and Glu.…

A: In the realm of enzymology, understanding the specificity of proteases is crucial for unraveling…

Q: Parts of the mechanism for lysozyme are shown below. The catalytic lysozyme residue side chains can…

A: Lysozymes cleave the  glycosidic bond between N-acetylmuramic acid (Mur2Ac) and N-acetylglucosamine…

Q: The figure shows an example of a thermal denaturation plot. The melting temperature (Tm) is the…

A: The proteins re folded into their proper three dimensional structure and this folding is driven by…

Q: c) A lysine residue in the active site of UstD is involved in forming a covalent Schiff base linkage…

A: UstD is an enzyme that decarboxylates specific acidic amino acids and allows the transfer of the…

Q: The enzymatic activity of lysozyme is optimal at pH 5.2 and decreases above and below this pH value.…

A: The enzyme lysozyme cleaves the glycosidic bond that connects N-acetyl muramic acid with the N-…

Q: The diagram below shows the substrate binding cleft for a protease, providing the substrate…

A: Proteases are enzymes which digest the proteins by cleaving the peptide bonds at specific locations.…

Q: (c2) Identify the active site residues that make hydrogen bonds and electrostatic interac- tions…

A: In order for an enzyme to properly bind its substrate and catalyze the reaction, several binding…

Q: A family of proteins known as cupredoxins contain a single redoxactive Cu ion coordinated by a Cys,…

A: Proteins are macromolecules or large biomolecules. Protein contains one or more long chains of amino…

Q: Consider a protein with two surface-exposed histidine residues: HisA is a “typical” histidine…

A: The Henderson-Hasselbalch equation for the deprotonation of a species is given…

Q: The trypsin enzyme is able to hydrolyze a peptide substate at the carboxyl side of an Arg or Lys…

A: Enzymes are protein molecules that increase the rate of enzyme reactions by decreasing the…

Q: Consider a protein with two surface-exposed histidine residues: HisA is a “typical” histidine…

A: The Henderson-Hasselbalch Equation for the deprotonation of a species is given below. pH= pKa +…

Q: . The allosterically regulated enzyme ATCase binds aspartic acid as a substrate and acylates the…

A: The allosterically regulated enzyme ATCase binds aspartic acid as a substrate and acylates the…

Q: Briefly describe the induced-fit conformational change when hexokinase binds its substrate.

A: Hexokinase is considered as the catalytic enzyme, which is involved in the glycolysis process.

Q: When starved, bacteria produce the intracellular signaling molecule ppGpp…

A: When prokaryotes and certain plants become nutritionally deficient, amino acid starvation is a…