Which strategies listed does this enzyme use to facilitate cleavage of α-galactoside? Choice 1 of 6:Dehydration synthesis Choice 2 of 6:acid base catalysis Choice 3 of 6:covalent catalysis Choice 4 of 6:metal ion catalysis Choice 5 of 6:stabilizing the transition state Choice 6 of 6:binding with high affinity to the product

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: If isolated regulatory subunits and catalytic subunits of ATCase are mixed, the native enzyme is…

A: ATcase (Aspartate transcarbamoylase) is an allosteric enzyme. It is involved in regulation of…

Q: You have discovered a new enzyme that has a nearly identical active site to chymotrypsin. This new…

A: As given peptide is Asn-Phe-lys, and discovered enzyme cleaves at C terminal of non ionizable polar…

Q: , non-ionizable R groups.

A: Introduction  Beginning with the first tetrahedral middle of the road, draw the instrument of…

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

A: ghhhhhhhhhhhhhhhhhhhhhhhhhhhhhhhhhhhhhhhhhhhhhhhhhhf vcxxxxxxxxxxxxxxxxxxxxxxxxxxxxxxxxxxxxxx

Q: relationship of the optimal pH and temperature on the absorbance value of enzyme…

A: The temperature increase or decrease with fixed pH, the absorbance decreases in enzyme activity…

Q: What is formed when serine 195 acts as a nucleophile on the carbonyl carbon of the peptide bond?…

A: A catalyst is a molecule that can increase the rate of a chemical reaction. The amount of catalysts…

Q: The enzyme lysozome catalysis the hydrolysis of polymer that consists of N-acetylglucosamine and…

A: Lysozyme is found in the secretions like tears, and sweat. It cleaves the beta 1-4 glycosidic bond…

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: 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: 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: Explain why several biochemical pathways start by putting a coenzyme A onto the molecule that…

A: For the functioning of an enzyme, a non-protein compound is usually needed. They loosely bind to…

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: List the components of the enzyme complex involved in the transition step   and  Simply describe…

A: Components of the enzyme complex :-

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

A: For regulation of A-ase: Feedback inhibition refers to the inhibition of the enzymes's activity by…

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

A:

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: co-factors in catalysis

A: Enzymes are protein that helps in catalyzing the chemical reaction. Some enzyme require a partner or…

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: 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: In a biochemical pathway where A--1--B--2--C--3--D. If D is a competitive inhibitor of enzyme 1,…

A: Answer: Introduction: Competitive inhibition is break down of a chemical pathway due to one chemical…

Q: Describe the features of the first binding site (for allosteric enzyme unprotkb-p39086), including…

A: Answer ::   Ligands are the molecules that bind to a receptor and change the confirmation of the…

Q: The rate constant for the uncatalyzed reaction of two molecules of glycine ethyl ester to form…

A: Given values: Rate constant in the uncatalyzed reaction = 0.6 M-1s-1 In the presence of catalyst…

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: 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: A type Il beta turn has what residue as one of the four residues that make up the turn? OAP O B. G O…

A: Ramachandran structure describes a protein all possible conformations.

Q: An example of an enzyme-catalyzed reaction proceeding via a transition-state stabilization mechanism…

A: Chymotrypsin is synthesized by the pancreas as inactive chymotrypsinogen. Chymotrypsin is a…

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: You have discovered a new enzyme that has a nearly identical active site to chymotrypsin. This new…

A: It is mentioned that the newly discovered enzyme with a reaction mechanism similar to that of the…

Q: Using the word anomeric carbon, “acceptor” nucleophilic substrate, and activated “donor”, describe…

A: In polysaccharides the monosaccharide units are linked by glycosidic linkages.

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 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: In what way is the observed mode of action of hexokinase consistent with the induced-fit theory of…

A: In enzymology, allosteric regulation is the inhibition or activation of an enzyme by a small…

Q: Is the reaction reversible Steps Structural Structural Formula activator and formula of the product…

A: Glycolysis is the cellular metabolic pathway where the six-carbon glucose molecule was hydrolyzed…

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: 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: How temperature, pH and salt affects the enzyme activity in terms of protein structure (primary,…

A: Most enzymes in cellular systems are protein molecules. They are biocatalysts that increase the…

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: Hb serves as our model for regulation of enzyme reaction rates. But Hb is not a Explain the…

A: Oxygen is required for the generation of ATPs in all the metabolically active cells of the body and…

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: Shown below is a proposed mechanism for the cleavage of sialic acid by the viral enzyme…

A: Neuraminidase belongs to the enzyme class hydrolase. It hydrolyzes the terminal sialic acid residues…

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: create a single illustration that will interrelate or link the two opposing pathways, the…

A: Answer :- The glycogenesis synthesis of glycogen from glucose in liver and muscles is known as…

Q: In the pentose phosphate pathway reaction that produces subtrate used for nucleiuc acid synthesis,…

A: The Pentose Phosphate Pathway is an anabolic pathway which is carried out to synthesize NADPH and…

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…