RuBP carboxylase is not an idel enzyme by any means. Describe some of the active site's and substrate specificity's issues. When the amino acid sequences of this enzyme from several species are compared, they are nearly similar. What importance does this homogeneity have?

Q: (a) What are the Vmax and Km (including units) for Tigerzyme? b) What are the Vmax and Km…

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

Q: Chymotrypsin is a pH dependent protein. Enzymatic activity is the greatest between pH=7.0 to pH=8.5.…

A: Chymotrypsin is a protease that is secreted by the pancreas. It cleaves the peptide bond next to the…

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

A: Introduction :- Enzymes are biological catalysts that accelerate chemical reactions in cells. They…

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: The substrate which was used to investigate the enzymatic activity of wheat bran phosphatase was…

A: Base was added so that pH will become high as it can show the pink color. If pH will not be high…

Q: In each case, these are enzymes that catalyze thesame reaction in different species. The question…

A: 1.Aminopeptidases (PR1A from mammal and PR1B from malaria parasite):First, obtain the…

Q: Using the catalytic mechanism of serine proteases, draw and label a reaction coordinate…

A: In order to draw the reaction coordinate diagram of the chymotrypsin catalyzed hydrolysis of a…

Q: The amino acid histidine has been found to participate in both acid and base catalysis in many…

A: Histidine is a basic amino acid and it contains an imidazole ring in its side-chain. Histidine is…

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: Carbonyl cyanide 4- ( trifluoromethoxy ) phenylhydrazone (FCCP) is a proton ionophore : it enables…

A: E.coli uses the protons to drive against the lactose gradient. Moreover, E.coli is a secondary…

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: 3CLpro is a cysteine protease, which are among the most common proteases in biochemistry, however…

A: The 3 dimensional conformation of a biomolecule is highly specific and vital to its function,…

Q: What class does your HindIII enzyme belong?

A: HindIII is a restriction endonuclease (RE).

Q: Using the biosynthesis of aminolevulinate (ALA) as an example, describe at least two techniques that…

A: Biosynthesis of aminolevulinate (ALA): ALA is a biomolecule synthesized using the ALA synthase…

Q: In the Lineweaver Burke plot shown below, which of the following is true? Wth inhto Wthout inhittor…

A: Since there are multiple questions and which question is to be solved has not been specified, as per…

Q: What is the step by step process Embden-Meyerhoff-Parnas pathway? Can you please explain in detail…

A: After glucose enters the cell, there are two possible fates it can undergo: enter glycolysis, where…

Q: X-ray crystallographic studies of ATCase in the R form required the use of the bisubstrate analog…

A: ATCase (Aspartate Transcarbamoylase) is an enzyme regulated allosterically with unique quaternary…

Q: Tazobactam is a BETA-lactam that inhibits the enzyme that bacteria secrete to resist penicillin

A: Tazobactam is a synthetic sulfone of penicillanic acid which contains a lactam ring at beta…

Q: In the Avery experiment, mice were killed if they injected with S strain cells. Furthermore,…

A: Griffith's experiment, reported in 1928 by Frederick Griffith was the first experiment suggesting…

Q: For answer (a) regarding the last row of compounds, why is the -CH-(CH3)2 not also responsible for…

A: Proteases are enzymes that cleave peptide bonds that link two amino acid residues together.…

Q: Bovine chymotrypsin is a serine protease.  The enzyme is structurally stable over the pH range of…

A: Chymotrypsinogen enzyme is responsible for the activation of trypsinogen into trypsin during 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: Trypsin contains a/an [aspartate/serine/histidine] in its specificity pocket to attract lysine and…

A: Trypsin is an enzyme involved in the cleavage of peptide bonds at specific sites. In the pancreas,…

Q: In the: Presence of competitive inhibitors of peptidyl transferase. Explain: (a) What is the process…

A: The peptidyl transferase is an aminoacyltransferase and the ribosome's principal enzymatic function,…

Q: serine proteases act via a two-step catalytic mechanism. However, as a critical scientist, you may…

A: Serine proteases are protein cleaving enzymes that have Serine, Histidine and Aspartate (the…

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…

Q: The following data describe the catalysis of cleavage of peptide bonds in small peptides by the…

A: Peptide bond cleavage is the basic process of hydrolysis of a polypeptide where the peptide bond…

Q: Enzymes are stereochemically specific; that is, they oftenconvert only one stereoisomeric form of…

A: enzymes are proteins that are made up of amino acids. Enzymes contain active sites. These active…

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: Draw the amino acid–Schiff base that forms in the breakdown of 3-hydroxykynurenine to yield…

A: In enzymology, Kynurenine-3-monooxygenase also known as Kynurenine hydroxylase is an enzyme that…

Q: A lipase enzyme has been isolated from a bacterium with a strong red color, found in industrial…

A: Enzymes are protein molecules that increase the rate of reaction by decreasing the activation…

Q: please provide the structure of the enzyme's catalytic serine residue (as a monomer)

A: The catalytic serine residue in enzymes plays a crucial role in many biochemical reactions. The…

Q: Chymotrypsin is a digestive enzyme with a catalytic optimum between pH 7.8 and 8.0. However, due to…

A: Henderson-Hasselbalch equation relates pH, pKa and the ratio of  concentrations of protonated to…

Q: Consider the metabolic pathway show below that converts substrate A to B with the enzyme B to C with…

A: When the binding of one ligand strengthens the attraction between substrate molecules and other…

Q: cytosol but those without this substance have concentrations of up to 50uM in the cytosol by the…

A: OmpF porin is a type of nonspecific protein that forms the pore at the outer membrane of bacteria…

Q: Describe the nitrogenase complex. How is the enzymeorganized? What are its unique components?

A: Nitrogenase complex constitutes dinitrogenase reductase which is an iron-sulphur protein,…

Q: Consider the Ramachandran plot to answer both questions. Which observation most likely describes…

A: The proteins are polypeptide chains of amino acids. These amino acids are packed into protein…

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…