Catalysis through proximity and orientation effects involves: (select all that applies) Group of answer choices binding of acidic and/or basic groups in the binding site facilitating chemical reactions by binding substrates close to specific groups binding of substrate in specific, restrictive orientations depending on metal ions for catalysis

Q: PMSF is a molecule used in biochemical research. It inactivates serine proteases by binding…

A: PMSF is phenylmethylsulfonyl fluoride which is a serine protease inhibitor.  Competetive inhibitors…

Q: Which of the following statements is TRUE considering SECONDARY metabolites:   a. Synthesized…

A: The correct option is (b) They are largely of medicinal use

Q: Given the active site and reaction mechanism below, what is the mechanism of rreversible inhibition…

A: The mechanism followed by the given example is of Transition state analog Chemical compounds with a…

Q: Which of the following is false regarding Serine Proteases? O They employ general acid-base…

A: Answer is a.) they employ general acid base catalysis.

Q: Indicate whether each of the following statements about enzyme terminology is TRUE or FALSE. All…

A: All defined enzymes are basically proteins. For its catalytic activity to be exercised, many enzymes…

Q: Where do each of these 5 main themes occur in the chymotrypsin mechanism?

A: Chymotrypsin is also called a serine protease as it has a serine residue in its active site. Ser-195…

Q: Protease is an enzyme that catalyzes the breaking of amide bonds which is very stable at “mild”…

A: The reaction mechanism which follows general acid-base catalysis is as follows.:

Q: complete the following mechanism showing the cleavge of the peptide bond for the following cysteine…

A: ghhhhhhhhhhhhhhhhhhhhhhhhhhhhhhhhhhhhhhhhhhhhhhhhhhf vcxxxxxxxxxxxxxxxxxxxxxxxxxxxxxxxxxxxxxx

Q: How many molecules of urea can one molecule of urease act on in 12.0 min ?

A: Number of molecules of urea in one molecule or urease act on in 12.0 min is given below in the 2nd…

Q: Circle and label one place on the mechanism where covalent catalysis is occurring. Suggest an amino…

A: Glycolysis is a catabolic breakdown of Glucose into pyruvate which consist of 10 metabolic steps. so…

Q: Given the active site and reaction mechanism, identify the mechanism of irreversible inhibition for…

A: Irreversible inhibition is a process in which inhibitors bind covalently or non-covalently to 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: Given the active site diagram and reaction mechanism, indicate the mechanism of irreversible…

A: Inhibition is of 2 type; Reversible inhibition and Irreversible inhibition. It is said that the…

Q: Define enzyme inhibition. Explain in detail the different types of inhibitions with suitable…

A: There are a variety of molecules that can inhibit or stimulate enzyme activity, as well as a variety…

Q: Catabolic and anabolic pathways are not identical as some enzymes function in only one direction.…

A: Metabolic pathways are a series of chemical reactions that are involved in either synthesis or break…

Q: Mechanisms of catalysis: Electrostatic catalysis         summary + example

A: Catalyst is a substance that helps in the process of catalysis. This substance is characterized by…

Q: Given the active site and reaction mechanism below, what is the mechanism of irreversible inhibition…

A: The given example is uncompetitive inhibition. Uncompetitive inhibition, also known as…

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

A:

Q: To purify a given enzyme from a crude extract that contains it, fractional precipitations, exchange…

A: Protein purification is necessary to purify the protein to homogeneity. Homogeneous protein sample…

Q: Which option is true about Chymotrypsin mechanism of action? Must select all true options. No part…

A: Chymotrypsin is an enzyme which helps in the digestion of protien and is  secreted by the intestine…

Q: mation of a Schiff base in the enzymatically catalyzed decarbox

A: Catalysis is a kind of process where the rate as well as the result of the reaction is affected by…

Q: You are trying to confirm that an enzyme you are studying has the following amino acid in its active…

A: Covalent modifications of amino acids involves the addition or removal of chemical groups to the…

Q: Complete the following table by providing the reactants/substrates, enzymes and their functions as…

A: Fatty acids are the major building blocks of the fats in the human body. It is a carboxylic acid…

Q: Rank these substrates in order of best inhibitor (highest binding affinity) to worst inhibitor…

A: Ki is the inhibitor constant, that tells how potent an inhibitor is. It gives an idea of the…

Q: Compounds I, II, and III are in the following biochemical pathway: precursor compound I enzyme A…

A: Cell biology is considered as the study of cells, their structure, and their functions. The cells…

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

A: Chymotrypsin is a proteolytic enzyme acting in the digestive systems of many organisms. It…

Q: Rhodium and other transition metals are generally used in heterogeneous/homogeneouslenzyme…

A: Enzymes are the biocatalyst which promotes the biochemical reactions in any living organism. The…

Q: Żymogens are NOT enzymatically active, because O A. they are not yet shaped such that essential…

A: Enzymes are biological catalysts that are mostly made up of proteins that alter or increase the rate…

Q: Describe the mechanism of catalysis Thiamine Pyrophosphate (TPP), (Vit. B1) Pyridoxal Phosphate…

A: Introduction: The substance that increases the rate of the chemical reaction without changing itself…

Q: Enzymes can: make exothermic reactions into endothermic reactions. change the direction of a…

A: Enzymes are proteins that helps to accelerate chemical reactions by binding to substrates and…

Q: When the final product of a series of enzymatically-catalyzed reactions binds to the first enzyme in…

A: Enzymes are the biocatalyst which are responsible for enhancing the rate of a reaction by decreasing…

Q: 19. Define the terms “cofactor” and “coenzyme.” 20. What is the difference between general acid-base…

A: Enzymes are biocatalysts that speed up the reaction. Enzymes decrease the activation energy of a…

Q: i) Explain the pH dependence of lysozyme catalysis shown in the Figure 1 below 100 50 4 8. 10 pH…

A: Lysozyme It is enzyme which is found in secretions of body like tears, mucus, saliva, etc. This…

Q: Given the active site diagram below, identify the acidic residue from the indicated components.

A: Amino acids are basic unit for any protein or polypeptide chain. It consist of -COOH, -NH2, side…

Q: Given the active site and reaction mechanism below, what is the mechanism of irreversible inhibition…

A: Introduction: Substances that interfere with the enzyme activity are called inhibitors. It is…

Q: Which one of the following statements does NOT correctly describe the current state of the…

A: Chymotrypsin is synthesized in the pancreas. Chymotrypsin is the serine protease. In the active site…

Q: The apo form of an enzyme: (select all that applies) Group of answer choices Is the cofactor-free…

A: Enzymes are biological catalysts which can only function in specified pH, pressure, and temperature…

Q: Populate the table with expected results using color codes (-), (+), (++), and (+++). Table 3.…

A: Polyphenol oxidases are enzymes having copper has its prosthetic group, it have both tyrosinase and…

Q: Describe the experimental evidence that supports lysozyme’s catalysis by acid– base catalysis,…

A: Lysozyme, also known as muramidase or N-acetylmuramide glycanhydrolase, is an antimicrobial enzyme…

Q: Match the pair of words with the description of the difference between them. Negative allosteric…

A: Enzyme inhibitors are defined as molecules or compounds that bind to an enzyme and affect their…

Q: Triclosan is a broad-spectrum antibacterial agent used in many household products. It is…

A: Anti-bacterial agents are chemicals that have the ability to kill bacteria and limit their growth.…

Q: Enolase has a glutamic acid residue in its active site. Describe the experiment that was done that…

A: Enolase is a metalloenzyme used in the 9th step of glycolysis it other name is PG i.e…

Q: With a ∆G°´ of -16.7 kJ/mol, the reaction catalyzed by hexokinase is considered to be _____. at…

A: Hexokinase is a phosphorylating enzyme that catalyses the transfer of phosphate group from ATP to…

Q: 200 ml of a 2% protein solution are available, containing an enzyme to be purified. Half of the…

A: Protein is a macromolecule made up of monomers aminoacids.  Protein helps maintain the structural…

Q: Given the active site diagram below, indicate the mechanism(s) of catalysis. 5 HO OH HN OH *HN NH…

A: The figure in question shows the mechanism of formation of transition state. By analyzing the active…

Q: Please discuss the following statement. "If two ligands involve in the same number and type of…

A: Asked : Statement is true or false

Q: Mechanisms of catalysis: 2.3 Covalent catalysis  summary + example

A: Enzymes are macromolecular biological catalysts that accelerate chemical reactions. The molecules…