What is formed when serine 195 acts as a nucleophile on the carbonyl carbon of the peptide bond? What catalytic mechanism(s) is/are at play here?
Q: What is the difference between an enol phosphate and a normal phosphate ester that gives PEP such a…
A: High energy compounds are molecules that, on hydrolysis, release a high amount of energy, such as…
Q: A point mutation in Hb diminishes hydrophobicity at the heme. Which of the following impacts would…
A: Hb hemoglobin carries O2 in the blood during the gaseous exchange.
Q: Considering the general structure of penicillins, how are they rendered ineffective? Select one: O…
A: •Penicillin nucleus consists of fused Thiaolidine and B- Lactam linkage to which side chains are…
Q: complete the following mechanism showing the cleavge of the peptide bond for the following cysteine…
A: ghhhhhhhhhhhhhhhhhhhhhhhhhhhhhhhhhhhhhhhhhhhhhhhhhhf vcxxxxxxxxxxxxxxxxxxxxxxxxxxxxxxxxxxxxxx
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: 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: While R256T and K364R are at different positions, both mutations are present in the active site.…
A: Two substitution mutations are made in the active site of the given protein or enzyme. The active…
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: Do you think that catalase should be able to attach to other substrates besides H2O2? Why or why…
A: Catalase is an enzyme that catalyzes the reaction by which hydrogen peroxide is broken down into…
Q: This question should be answered with two or three sentences using relevant biochemical vocabulary.
A: Serine endopeptidases or serine proteases are enzymes with nucleophilic serine at active sites which…
Q: The enzyme chymotrypsin, catalyses the hydrolysis of nitrophenyl acetate and pther acyl esters. Name…
A: Chymotrypsin is a digestive enzyme belonging to a super family of enzymes called serine proteases.…
Q: Considering the general structure of penicillins, how are they rendered ineffective? Select…
A: Penicillin is an antibiotic that inhibits the formation of peptidoglycan cross-links of the…
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: 16. This figure from Foundations should look familiar. Which protein is shown here? catalytic triad…
A: Every enzyme has its own active site where substrate molecules bind and undergo a chemical reaction.…
Q: The enzyme lysozyme hydrolyzes glycosidic bonds in peptidoglycan, an oligosaccharide found ir…
A: Enzymes are the biocatalysts that are specific for the substrate binding to carry out all the…
Q: Which of the following amino acids can act as nucleophiles in a protease active site (choose all…
A: Enzymes are biocatalysts that can speed up the chemical reactions taking place in the living system.…
Q: If you were to mutate Ser195 in the catalytic triad of chymotrypsin to another amino acid, which…
A: A change in the nucleotide sequence is referred to as a mutation. A mutation in the nucleotide…
Q: Why is it advantageous for two control mechanisms —allosteric control and covalent modification— to…
A: Enzymes are the proteins which act as a catalyst in chemical reactions. Enzymes never take part in…
Q: What are the biomolecules that are used to biosynthesize a purine ring in the de novo pathway –…
A: Purine synthesis occurs in liver by two pathways i.e denovo synthesis and salvage pathway. Denovo…
Q: Looking at the structure of RDV-TP, what changes in the structure of the molecule does the active…
A: The building blocks of DNA and RNA are purine and pyrimidin. Purine are heterocyclic compound.…
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: Chymotrypsin, trypsin, and elastase all share the same catalytic mechanism, but have different…
A: Proteases are enzymes that cleave polypeptide chains. They all hydrolyze the peptide bond present in…
Q: for GABA transaminase, ornithine decarboxylase, and alanine
A: PLP-dependent enzymes catalyse a wide range of reactions that result in bond cleavage at the carbons…
Q: Under normal circumstances, serine residues are not very reactive. How can serine 195 be used as a…
A: Nucleophiles donate electrons and electrophiles gain electrons. Usually, serine residues do not…
Q: In addition to the reactions mentioned in Section 23.5, PLP can catalyze b-substitution reactions.…
A: Pyridoxal phosphate (PLP) is a coenzyme for a variety of enzymatic biochemical reaction. PLP is the…
Q: Which of the following statements about ribozyme catalytic residues is INCORRECT? General acid…
A: Solution :- the ribozyme Catalytic residues which are RNA molecules and it's fuction as chemical…
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 peptide bond on the C=O side of bulky hydrophobic residues is cleaved by a) Trypsin b) RNase H…
A: Proteins are long-chain peptides formed of amide bonds (also known as peptide bonds) between the…
Q: Catalytic residues are often found in loops between helices or strands for increased mobility during…
A: The amino acids that are known to be involved in the chemical reaction catalyzed by an enzyme are…
Q: What step ends the first-half of the chymotrypsin mechanism? Attack of water on the acyl-enzyme…
A: Chymotrypsin is a proteolytic enzyme secreted by the pancreases in the small intestine.
Q: Name the three amino acids (AA) intermediate in the urea cycle. 2. What are the four…
A: Urea cycle is a series of biological reactions in which ammonia is converted into urea. Urea cycle…
Q: the structures of chymotrypsin and other serine proteases revealed that the active sites of these…
A: Chymotrypsin and trypsin are examples of serine proteases. Chymotrypsin cleaves the peptides of…
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: Consider applying biocatalytic reduction with carrots to the following two ketones: tert-butyl…
A: Introduction :- Bio-catalysis is the process of using natural substances like- enzymes for…
Q: Which substrate is the best substrate for chymotrypsin? O N-acetylphenylalanine ethyl ester with Km…
A: Chymotrypsin is a digestive enzyme component of pancreatic juice acting in the duodenum where it…
Q: The chemical structure of Coenzyme A contains the following EXCEPT— a β-mercaptoethylamine…
A: The correct answer is LIPOIC ACID RESIDUE
Q: catalytic function of C25
A: Protease is one of several enzymes that hydrolyze the proteins. They cut the peptide bond which…
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: 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: 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: The oxyanion hole is comprised of hydrogen bonding atoms that project into a space on the active…
A: Oxyanion hole is generally found in proteases and are located in catalytic site of enzymes.…
Q: 1. Depict the structure features in the active site of cysteine protease 2. provide a step-wise…
A: Cysteine protease is a papain family enzyme.
Q: Give a possible set of bacterial factors (or lack thereof) and what properties they have that would…
A: 50% inhibitory concentration is the concentration of drug required for inhibiting 50% bacterial…
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 is the evidence that ATCase has distinct regulatory and catalytic sites?
A: Introduction: Aspartate transcarbamoylase(ATCase) is the enzyme that catalyzes the first reaction of…
Q: Why is the covalent intermediate of elastase stable at low pH? The catalytic histidine cannot act as…
A: Elastase is an enzyme which is a serine protease. It contain ser, his and asp in its catalytic…
Q: Using the word anomeric carbon, “acceptor” nucleophilic substrate, and activated “donor”, describe…
A: The oligosaccharides are formed by connecting monosaccharides via glycosidic linkages.
Q: what is meant by S195? D102? H57?
A: S195,D102 and H57 are catalytic triad which is present in chymotrypsin enzyme. The active site of…
- What is formed when serine 195 acts as a nucleophile on the carbonyl carbon of the peptide bond? What catalytic mechanism(s) is/are at play here?
Trending now
This is a popular solution!
Step by step
Solved in 3 steps
- The oxyanion hole is comprised of hydrogen bonding atoms that project into a space on the active site that will have all H-bonding potential satisfied only during the catalytic cycle of the reaction. True or False? The catalytic triad residues are all next to each other in the primary sequence of trypsin. True or False?What is the catalytic triad on chymotrypsin? Detail its importance.An inhibitor that specifically labels chymotrypsin at histidine 57 is N-tosylamido-l-phenylethyl chloromethylketone. How would you modify the structure of this inhibitor tolabel the active site of trypsin?
- An inhibitor that specifically labels chymotrypsin at histidine 57 is Ntosylamido-l-phenylethyl chloromethyl ketone. How would you modify the structure of this inhibitor to label the active site of trypsin?The oxyanion hole deprotonates an incoming water molecule to convert it to a potent nucleophile. True or False? The oxyanion hole is comprised of hydrogen bonding atoms that project into a space on the active site that will have all H-bonding potential satisfied only during the catalytic cycle of the reaction. True or False? The catalytic triad residues are all next to each other in the primary sequence of trypsin. True or False?What kind of inhibitor is threo-sphingosine? Explain this type of inhibition.
- The catalytic triad consists of Asp, His, and Ser. What would be an alternative for histidine and how would we draw the interactions in a mechanism?How would chymotrypsin's catalytic triad be affected by extremely low and extremely high pH values (assuming the rest of the protein remains intact)?UDP-glucuronosyltransferase enzymes bind the organic compound UDP-glucuronic acid (UDP-GA) in order to catalyse the transfer of a glucuronic acid group from UDP-GA to a drug molecule, releasing UDP from the active site as a product. UDP is then regenerated by the activity of another enzyme. What terms could be used to describe UDP-GA?
- Are any of the intermediates in the β-oxidation pathway chiral? Explain.Draw a schematic illustration of the hydrolysis of N-acetylphenylalaninamide catalyzed byalpha-chymotrypsin in which you indicate the important catalytic residues in the active site and how thesubstrate undergoes transformation to products through two different tetrahedral intermediates.How can we test the validity of the mechanism proposed for the catalytic triad?