Which one is the most likely to be a catalytic triad of an enzyme that follows general acid base catalysis?
Q: Some of the following four amino acids : alanine, arginine, histidine, aspartic acid would provide a…
A: Acid-Base Catalysis is involved in the reaction mechanisms that requires the transfer of a proton…
Q: Draw the tripeptide val-glu-his as it exists under physiological pH. Write the reaction for the…
A: A peptide bond is an amide linkage formed between two molecules where an α-carboxyl group of one…
Q: Each of the amino acid residues in the catalytic triad is part of what polypeptide chain?
A: The enzymes carry out the catalysis of various reactions in metabolism. The catalytic triad helps…
Q: When a nonapeptide undergoes partial hydrolysis, it forms dipeptides, a tripeptide and two…
A: Amino acids are the simplest units to form a peptide or a protein. The peptide or protein sequencing…
Q: Histidine is frequently used as a general acid or base in enzyme catalysis. Considering the pKa…
A: Histidine is an essential amino acids with unique acid / base properties. -It is a precursor of…
Q: Identify the amino acid residue, nucleophilic catalytic residue and which of the catalytic residue…
A: Chymotrypsin is a type of protease enzyme. It acts as a digestive enzyme, primarily synthesized in…
Q: Match the following tripeptide with its given characteristic: contains sulfur? 1. Tyr-Lys-Met…
A: Amino acids are organic compounds that contain a carboxyl group, an amino group, a hydrogen atom and…
Q: conjugate base of the weak acid, CH3COOH in an acid b ace action?
A:
Q: What enzyme class do each of the following reactions belong to. Do not give specific enzyme names,…
A: Enzymes are the biocatalysts which speed up the reactions. These do so by providing lower activation…
Q: Which of the following amino acid residues would not participate in general acid-base catalysis? A.…
A: Acid-base catalysis is the reaction mechanism that deals with the transfer of a proton from one…
Q: To what main enzyme class do the enzymes that catalyze the following reaction belong?…
A: Introduction: Those substances that increase the pace of the reaction without undergoing any change…
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: Draw all possible products of a single hydrolysis being completed on the following polypeptide:…
A: Hydrolysis of protein peptide is the breaking down the peptide bond by addition of water molecule.
Q: he slowest step in a multi-enzyme pathway is called the------------
A: The slowest step in a multi-enzyme pathway is called the-------------- the rate-determining step…
Q: When free water molecules are excluded from an enzyme’s catalytic pocket, is a catalytic −OH group…
A: Enzymes are the catalytic protein, which has the active site to bind with the substrate and result…
Q: Which of the following is the most probable catalytic triad of an enzyme that follows general acid…
A: The active site of several enzymes has a catalytic trio, which is a group of three coordinated amino…
Q: Given the active site diagram below, please identify the residue participating in a charge-charge…
A: Note- we are supposed to answer one question according to our guidelines. Please repost the other…
Q: NH он NH2 LOH OH O NH, NH но HN OH HN NH2 NH он ÔH HN. OH NH HN NH2
A: Oligopeptides are also referred as peptide. Oligopeptide consists of 2 to 20 amino acids.
Q: What is the name of the prosthetic group in the image , In the left image the prosthetic group is…
A: Enzymes are biological catalysts that help in catalyzing or speeding up biological reactions by…
Q: The amln0 acid histldine ls usually found in actlve sltes 0f enzymes. What structural feature does…
A: Enzymes are protein molecules that increase the rate of reaction by decreasing the activation energy…
Q: Which step in lipid metabolism would you expect to be affected by 3,4-dihydroxybutyl-1-phosphonic…
A: Lipid metabolism is the synthesis and degradation of lipids in cells, involving the breakdown or…
Q: Within an enzyme active site, how does the aspartate carboxyl group activate the histidine nitrogen…
A: An enzyme is a special class of proteins that catalyze biochemical reactions. Proteolytic enzymes…
Q: H2C HO CH2 H. N. CH H2C. Enzyme X is an aspartyl protease. Here is the tetrahedral intermediate in…
A: Aspartyl proteases are proteases that contain two conserved aspartic acid residues at the active…
Q: On Catalase, what is the optimum pH and temperature of the enzyme?
A: Enzymes are familiarly known as the catalysts in a reaction which play a crucial role in enhancing…
Q: Which of the following amino acid residues cannot play a role in acid-base catalysis? a. Aspartate…
A: Acid-Base Catalysis is reaction process involving the movement of a proton from one molecule to…
Q: The formation of the acyl-enzyme complex in chymotrypsin is through a ------------- reaction between
A: Enzymes are known as biological catalysts that help to catalyze the different biochemical reactions…
Q: Help me, please
A: Proteases are enzymes that catalyze the breakdown of the peptide bonds in the protein. Serine…
Q: Draw the glycosphingolipid with a head group (as Hawortn B-D-GalNac-(1->3)-B-D-Glc-Sphingolipid. For…
A: Glycosphingolipids are mostly found in the cell membrane of the central nervous system. These are…
Q: the complete hydrolysis of this compound gives and -- (Write the amino acids name in three-letter…
A: A protein is made up of a polypeptide chain made up of Amino acid.
Q: In the chemical mechanism of chymotrypsin, the group that acts as a general base in the deacylation…
A: Hi! Thanks for your question. As you have posted multiple questions and have not mentioned which one…
Q: For the chemical reaction that results in the formation of a peptide bond between two amino acids,…
A: The peptide bond is formed when the two amino acids are joined together with the release of water…
Q: What structure deactivates the enzyme that catalyses the following reaction? de de do Per O The…
A: G protein-coupled receptors can be grouped into three main categories namely the Gq, the Gs, and the…
Q: s N-acetyl-β-D-glucosamine a reducing sugar? What about D-gluconate? Is the disaccharide…
A: Any carbohydrate with an aldehyde or a hemiacetal in equilibrium with an aldehyde in its structure.…
Q: The interconversion between the two forms of guanine base shown below is called form of guanine is…
A:
Q: What is the ratio of [A-]/[HA] in a solution with pH = 11.5? NH3 sh NH₂ sh + H+
A: Lysine is a basic amino acid with an amino group in its side chain. The pKa value of the lysine side…
Q: When glucose is reduced, only one alditol is produced. When fructose undergoes the same reaction,…
A: Introduction: Reducing sugars are those sugars that have a free aldehyde or ketonic group. When…
Q: What is a potential disadvantage of having many catalytic sites together on one very long…
A: A catalytic site is the small, high conserved constellation of residues within the active site that…
Q: What classification of enzyme is catalase? Give the Enzyme Commission (E.C.) number of catalase.
A: Enzymes are biocatalysts that increase the rate of the chemical reaction without undergoing any…
Q: In many cases, the wrong residue at the active site of a protein will result in a non- functional…
A: Most of the enzymes are proteins. The enzymes have an active site to which the substrate molecule…
Q: What fragments can be generated in the decapeptide Gly-Lys-Ala-Met-Gly-Gly-Phe-Tyr-Trp-Ala if is…
A: Note: it is assumed that the left side of the sequence is the N terminal and the right side of the…
Q: Which step in lipid metabolism would you expect to be affected by 3,4-dihydroxybutyl-1-phosphonic…
A: Lipid metabolism is the synthesis and degradation of lipids in cells, involving the breakdown or…
Q: H2N NH3 HO, H,O H2N. NH2 СООН COOH glutamic acid glutamine why does the reaction not proceed?
A: Amino acids are units that synthesize proteins. Amino acids are synthesized by ribosomes. The…
Q: Which statement correctly explains the protonation states of these histidine residues? O His side…
A: Most acid molecules are deprotonated when the pKa is lower than the pH. When pH is equal to the pKa,…
Q: To which enzyme class do these enzymes and reactions belong? Label each as oxidoreductase,…
A: An enzyme is a catalyst that speeds up a chemical reaction in the cells. Enzymes are almost proteins…
Q: Identify the enzyme needed in each of the following reactions as an isomerase, a decarboxylase, a…
A: Enzymes have common names which help to predict about the reactions that are catalyzed by the…
Q: Draw out the steps in the synthesis of the dipeptide Ala–Gly.
A: A peptide is a compound consisting of two or more amino acids. When two amino acid molecules are…
Q: Some of the following four amino acids : alanine, arginine, histidine, aspartic acid would provide a…
A: Introduction: Acid-base catalysis is a mechanism in which the transfer of a proton from an acid…
Q: Using the following data, determine the correct sequence of the octapeptide. Edmund's Reaction =…
A: Chains of Amino acids are held together through a peptide bond to form a structure known as…
Step by step
Solved in 2 steps
- Which of the following is the most probable catalytic triad of an enzyme that follows general acid base catalysis? -Glu-His-Cys -Leu-His-Ser -Glu-Phe-Ser -Asp-His-Ala -Glu-Phe-Ser -Glu-Phe-Ser -Glu-Phe-Ser -Glu-Phe-Ser -Glu-Phe-Ser -What amino acid(s) is(are) deemed to be present when a positive reaction is obtained upon heating in a 40% NaOH and 2% lead acetate? cysteine and methionine methionine and cystine cystine and cysteine cysteine, cystine, and methionineIn a biochemical reaction that involves the substrate urea and the liver enzyme urease, decreasing the pH by one unit from its optimum value will _______ the rate of enzyme activity.
- Each of the amino acid residues in the catalytic triad is part of what polypeptide chain?What effect does the optimum pH and temperature have on enzyme function? Briefly explain with an example no plagiarismHow many moles of active sites are there in 1 mg of enzyme? Assume that each subunit has one active site.
- What effects does pH have on enzyme activity? Cite relevant experimental data. How can you explain this relationship(cause)?Is the formation of a serine ester an example of acid/base catalysis, group transfer or electrostatic stabliziation?In each of the following pairs of amino acids, identify which amino acid would be more soluble in water: (a) Ala, Leu; (b) Tyr, Phe; (c) Ser, Ala; (d) Trp, His