The formation of the acyl-enzyme complex in chymotrypsin is through a ------------- reaction between
Q: Identify the enzyme that carry out the below reaction and denotes the nature of the enzyme?…
A: Oligomeric proteins are made up of two or more polypeptide chains that are connected to one another…
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: Streptokinase is engineered in the following way to make it resistant to protease O a. By replacing…
A: "Biotechnology" is the use of our knowledge of biological processes to the development of beneficial…
Q: Which class of enzymes catalyzes the following reactions? CH2 CH2- CH2 AST CH2- CH2 CH-NH + c=0 + +…
A: Enzymes are protein molecules that increase the rate of reaction by decreasing the activation energy…
Q: Which of the following is not a top category for enzymes according to the International…
A: The human body consists of a huge network of various cells, tissues, organs, and glands. All of them…
Q: What is the activated reactant in the biosynthesis of each of the following compounds? a.…
A: a. Phosphoribosylamine is an intermediate in purine metabolism. c. Orotidylate is a pyrimidine…
Q: The formation of a peptide bond between two amino acids is an example of a(n) _____ reaction.
A: During polypeptide synthesis the amino acids are joined together by peptide bond and the peptide…
Q: Which of the following is NOT a catalytic strategy used by trypsin? a. Acid-base catalysis b.…
A: Enzymes require an ideal pH range and temperature to operate properly. The tertiary structure of the…
Q: The Krebs cycle is considered to be an anabolic pathway because some of the reactions are
A: Krebs cycle: Krebs cycle also know as TCA cycle or citric acid cycle is an important part of aerobic…
Q: Hexokinase is an example of a general class of enzymeknown as the _____________________.
A: Hexokinase is an enzyme that phosphorylates hexoses forming hexose phosphate.
Q: In gluconeogenesis, a very specific enzyme with one and only one substrate removes the phosphate…
A: Introduction: Gluconeogenesis is the synthesis of glucose from non-carbohydrate compounds and mainly…
Q: The amino acids glutamine and glutamate are central toamino acid metabolism. Explain.
A: The metabolism of amino acids plays a vital role in our body to aid various biological reactions.…
Q: What kind of reaction is catalyzed by each of the following enzymes? a. citrate decarboxylase b.…
A: An enzyme is a substance that acts as a catalyst in living organisms, regulating the rate at which…
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: The enzyme threonine dehydrogenase which catalyzes one of the reactions in the production of the…
A: Enzyme threonine dehydrogenase is an enzyme, the amino acid isoleucine synthesized from it.
Q: The meat tenderizer used in cooking is primarily papain, a protease enzyme isolated from the fruit…
A: Tenderness of meat refers the quality of meat that easily cut or chewed. Due to the rigor mortis,…
Q: For the conversion of Trypsinogen into Trypsin, how many amino acids should be cleaved and from…
A: Given: For the conversion of Trypsinogen into Trypsin.
Q: The following enzymes belong to the same class of enzymes, except for A. Chymotrypsin B. Thrombin C.…
A: Enzymes are chemical substances which speed up the reaction process. There are many classes of…
Q: In transamination reactions, which of the following is not a donor amino acid–acceptor α-keto acid…
A: Transamination was the process in which amino group was removed from the amino acid and transfer…
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: The enzyme lactate dehydrogenase (LDH) is produced as an isozyme, which is a way to control the…
A: Lactate dehydrogenase (LDH) is an enzyme of the anaerobic metabolic pathway and is an oxidoreductase…
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: Is the formation of the acyl-enzyme complex a unimolecular (SN1) or biomolecular(SN2) reaction?
A: The most significant difference between a ketone/aldehyde and a carboxylic acid derivative is that…
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: Which of the following statements about folic acid is not true? a. Folic acid is activated by folate…
A: Folic acid is water-soluble vitamin B12 which was an essential nutrient necessary for protein and…
Q: fill in the blank with the correct term and explain why that term fits best to the following , one…
A: Enzymes are a class of proteins that act as biological catalysts. These proteins increase the pace…
Q: Which of the following are not one of the end products of pyrimidine catabolism? (A) NH3 (B) co2…
A: The synthesis of purine and pyrimidine nucleotides is one of the important specialized pathways of…
Q: What metabolic substrate is produced from the carbon atoms of each of the following amino…
A: Amino acids are organic molecules which act as the building blocks of proteins. During the…
Q: All the following amino acids produce an intermediate of the TCA cycle except Isoleucine Leucine…
A: TCA cycle or tricarboxylic acid cycle also known as Krebs cycle operates in the mitochondria
Q: The metabolic reaction pathway that is responsible for the generation of the most reducing…
A: Metabolic pathways are the series of chemical reactions that occur in the cells which synthesize and…
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: The enzyme chymotrypsin, catalyses the hydrolysis of nitrophenyl acetate and other acyl esters. Name…
A: Chymotrypsin is a protease that belongs to the class hydrolase. It is a serine protease due to the…
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: What is meant by the statement that a pathway is amphibolic?
A: There are various biochemical reactions that occur in each living organism. They are important for…
Q: Which of the following enzyme classes catalyze reactions in which two molecules become covalently…
A: Based on the reaction they catalyse , the enzymes are classified in different…
Q: Which of the following amino acid residues would not provide a side chain for acid- base catalysis…
A: Introduction: Nearly one-third of all known enzymes require metal ions for the catalytic activity…
Q: Consider the following reaction. CH₂-CH-COO-CH₂-C-Coo- он b Which group of enzymes catalyzes this…
A: The six functional classes of enzymes are hydrolases, oxidoreductases, lyases, transferases, ligases…
Q: What general kinds of reactions do the following types of enzymes catalyze?(a) Kinases (b)…
A: An enzyme accelerates the rate of a chemical reaction. The formation of enzyme-substrate complex is…
Q: If we describe an enzyme like aspartate transcarbamoylase and say that it exhibits cooperativity,…
A: Enzyme cooperativity is a phenomenon in which the shape of one subunit of an enzyme consisting of…
Q: In this process of enzyme inhibition, a molecule binds to a site on the enzyme that is NOT the…
A: An enzyme inhibitor are molecules that interrupt or decreases the rate of an enzyme catalyzed…
Q: ATP synthase is a protein that catalyzes the formation of the energy storage molecule adenosine…
A: Given: ATP synthase is the protein that catalyzes the formation of the energy storage molecule…
Q: The highest energy point of the serine protease reaction is the formation of the tetrahedral…
A: The serine protease reaction is a chemical reaction in which the enzyme breaks the peptide bond…
Q: give an example like the reaction mechanism of serin protease for example, with pictures & full…
A: Proteases are enzymes which cleave the peptide bonds and digest the proteins. Serine proteases are…
Q: In a particular enzyme,an alanine residue is located in a cleft where the substrate bonds.A mutation…
A: Introduction: The functional segment of hereditary material that mainly codes for the proteins is a…
Q: You have discovered a new enzyme that has a nearly identical active site to chymotrypsin. This new…
A: Enzyme catalyst is a substance that increases the rate of a chemical reaction without being consumed…
Q: In the reaction: glu-1-phosphate to glu-6-phosphate, what reaction is involved? Name the enzyme.…
A: Glycolysis is one of the major metabolic pathways in the body. Since glucose is the primary source…
Q: "which of the following can be used to replenish oxaloacetate in the krebs cycle" a. aspartic acid…
A: Replenishment of oxaloacetate in Krebs cycle: The concentrations of the intermediate molecules of…
Q: Which of the following is a degradation product of both cytidine and deoxycytidine? a. β-alanine b.…
A: Cytidine is a nucleoside molecule that is formed when cytosine is attached to a ribose ring via…
Q: Lysozyme catalyzes a "bi-bi" reaction, which means there are (how many) reactants and (how many)…
A: The reaction that is catalyzed by single enzyme and involves two substrates and two products is…
Q: What intermediate in purine synthesis will accumulate if a strain of bacteria is lacking each of the…
A: The pathways for the biosynthesis of nucleotides fall into two classes: de novo pathways and salvage…
The formation of the acyl-enzyme complex in chymotrypsin is through a ------------- reaction between.
Step by step
Solved in 2 steps
- The metabolic precursor for the production of most eicosanoids isWhy does the enzyme reaction for chymotrypsin proceed in two phases?Name the α-ketoacid that is formed by the transamination of each of the following amino acids: (a) Alanine (d) Leucine (b) Aspartate (e) Phenylalanine (c) Glutamate (f) Tyrosine
- The amino acids glutamine and glutamate are central toamino acid metabolism. Explain.true/false: Glutamine synthetase is responsible for the synthesis of glutamine from glutamate.Which of the following statements is not true about the catalytic triad in chymotrypsin? Group of answer choices the side chain of the serine 195 is hydrogen bonded to the imidazole ring of histidine the -NH group of the imidazole ring of histidine is hydrogen bonded to the carboxylate group of aspartate 102 the histidine residue serves to position the aspartate 102 side chain and to polarize its carboxylate group so that it is poised for deprotonation histidine acts as a general base catalyst none of these
- For the conversion of Trypsinogen into Trypsin, how many amino acids should be cleaved and from which site? Write down the sequence of these amino acids.All the following amino acids are converted to succinyl-CoA except Group of answer choices Lysine Methionine Isoleucine ValineAs a substituent, the hydrocarbon “tail” of the Ibuprofen molecule (see circle above) can be best described as n-butyl.  sec-butyl. isobutyl. tert-butyl
- It is absolutely not necessary to produce amylase in an active form in our body. But it is not in the case of trypsin. Given reasons.Why is trypsin an unusual name for an enzyme? (What is the convention for enzyme names?) .In blood type A, ___ is found at the nonreducing end of the oligosaccharide portion of the glycoprotein. a. N-acetylglucosamine b. α-D-galactose c. N-acetylgalactosamine d. L-fucose