Is the following statement correct or incorrect? It is only possible to employ enzymes that are present naturally in yeast or bacteria for biocatalysis.
Q: There is a cysteine protease, which uses a similar chemical mechanism to chymotrypsin except for…
A: Cysteine proteases are proteases that degrade protein and are also called thiol proteases. They use…
Q: Do our cells have own catalytic activity to mitigate the harsh effects of ROS? Elaborate
A: Ans: ROS: Reactive Oxygen Species are the molecules or chemicals which are responsible for…
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: 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 features distinguish enzymes that undergo allosteric control from those that obey…
A: Enzyme are the catalysts which increase the rate of reactions without affecting the equilibrium of…
Q: This is a linear biochemical pathway
A: Biochemical pathways is a step by step series of interconnected biochemical reactions in which each…
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: 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: What class does your HindIII enzyme belong?
A: HindIII is a restriction endonuclease (RE).
Q: Is the following true or false? Biocatalysis is limited to the use of enzymes found naturally in…
A: Biocatalysts are substances used in biochemical reactions. The biocatalysts are used to increase the…
Q: Comment on Figure 2a and Figure 2b regarding stabilization of the transition state and…
A: From the given energy diagrams; It is seen that the enzyme (E) and the substrate (S) at the start of…
Q: Genetic engineering of enzymes to be utilized for bioremediation efforts results in which of the…
A: Bioremediation is a process in which the organic wastes are biologically degraded under controlled…
Q: The primary structure of the enzyme lysozyme compared to its tertiary structure is an example of how…
A: Lysozyme is an enzyme present in the saliva and tear. It has an antibacterial effect. The substrate…
Q: Why is the Krebs cycle also called the final common pathway of the degradation of organic compounds?
A: Cellular respiration is the process by which the cells take the nutrients in the food and transform…
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: 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: two other enzymes that are used in therapeutic use in humans and why they do not affect human cells?
A: ENZYMES:- It is defined as a complex biological catalyst i.e produced by living organisms in its…
Q: A biochemical reaction will proceed in the direction as written if: Group of answer choices H > 0. G…
A: The thermodynamical properties such as free energy change, enthalpy change, and entropy change…
Q: Describe a common feature at the active site of serine proteases and acetyl cholinesterase
A: Acetylcholinesterase is an enzyme that catalyzes the hydrolysis of acetylcholine (which is a…
Q: Explain the basis for the following statement: As a coenzyme, pyridoxal phosphate is covalently…
A: Pyridoxal phosphate is the active form of vitamin B6. It is used as a coenzyme in a variety of…
Q: What is the definition of 1 unit of Taq polymerase activity according to a commercial supplier of…
A: Taq polymerase is a thermostable DNA polymerase I and is isolated from the thermophilic eubacteria…
Q: Enzymes are stereochemically specific; that is, they oftenconvert only one stereoisomeric form of…
A: enzymes are proteins that are made up of amino acids. Enzymes contain active sites. These active…
Q: What is the difference between pure and mixed noncompetitive inhibition?
A: Pure competitive inhibition is the type of inhibition in which the inhibitor binds to the site other…
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: Which strategies listed does this enzyme use to facilitate cleavage of α-galactoside? Choice 1 of…
A: Alpha-galactosidase enzymes are homodimeric glycoprotein which catalyzes the cleavage of terminal…
Q: What are the reasons for glucuronide conjugation being a major phase II metabolic route?
A: Biotransformation is a chemical modification of biomolecules like nutrients, amino acids, toxins and…
Q: What role do low-barrier hydrogen bonds play in serine protease catalysis?
A: A low barrier hydrogen bond is a special type of hydrogen bond which can occur when the pKa of the…
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: enzyme A enzyme B enzyme C compound 1 compound 2 compound 3 compound 4 Consider the biochemical…
A: The one gene one enzyme hypothesis is proposed by the Beadle and Tatum. George Beadle and Edward…
Q: An uncatalyzed reaction has a rate of 4.2 x 10-7 sec-1. When an enzyme is added the rate is 3.2 x…
A: Enzymes are proteins present inside organisms, which function to work as biological catalysts. These…
Q: Is it possible to envision models for the behavior of allosteric enzymes other than the ones that we…
A: Yes, it is possible to envision models for the behaviour of allosteric enzymes other than the ones…
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: How can we tell if the enzyme has been denatured by a particular temperature treatment.
A: Enzymes are proteinaceous molecules that act as catalysts in various cellular biochemical reactions.…
Q: The text states that in E. coli ribonucleotide reductase Tyrosine-122 was identified as the source…
A: Ribonucleotide reductase (RNR) is a key enzyme that mediates the synthesis of deoxyribonucleotides,…
Q: A Leu side chain can form Schiff base with the substrate during covalent catalysis. True False
A: Leucine is a hydrophobic amino acid with hydrophobic side chain. A schiff base is considered a…
Q: List the starting materials and cofactors required for IMP biosynthesis.
A: Inosinic acid or Inosine monophosphate (IMP) is a nucleotide or specifically ribonucleotide of…
Q: Please explain the functional role of decapping enzymes in prokaryotic cells?
A: The mRNA decapping complex is a protein complex in eukaryotic cells liable for evacuation of the 5'…
Q: if there are twelve different intermediate products produced in the stage of a metabolic within a…
A: Cellular metabolism is the set of metabolic reactions that occur in living organisms in order to…
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: The class of the enzyme catalyzing the reaction shown in this figure is a(n) Choose the one best…
A: Given, that the enzyme can catalyse the conversion of glucose to glucose-6-phosphate by transferring…
Q: Can you explain the following based on its mode of enzyme kinetics: 1) Synthesis/degradation of…
A: Regulation of metabolic reactions can be achieved by regulating enzyme activity. There are three…
Q: a biochemical pathway in which c02 is converted onto organic compounds
A: Carbon dioxide is a colorless gas and it is composed of carbon atom which is covalently double…
Q: What are the similarities and differences in the regulation of monomeric, single substrate and…
A: Monomeric enzymes are the one which have a single polypeptide chain like lysozyme and hexokinase…
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…
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…
Q: Mechanisms of catalysis: 2.3 Covalent catalysis summary + example
A: Enzymes are macromolecular biological catalysts that accelerate chemical reactions. The molecules…
Is the following statement correct or incorrect?
It is only possible to employ enzymes that are present naturally in yeast or bacteria for biocatalysis.
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- Pyridoxal phosphate (PLP) is a coenzyme for the enzyme ornithine aminotransferase. The enzyme was purified from cells grow in PLP = deficient media as well as from cells grown in media that contained pyridoxal phosphate. The stability of the two different enzyme preparations was then measured by incubating the enzyme at 37°C for different lengths of time and then assaying for the amount of enzyme activity remaining. The following results were obtained. (a) Why does the amount of active enzyme decrease with the time of incubation? (b) Why does the amount of enzyme from the PLP deficient cells decline more rapidly?Sydney Brennen isolated Salmonella typhimurium mutants that were implicated in the biosynthesis of tryptophan and would not grow on minimal medium supplemented with intermediates in tryptophan biosynthesis, some mutants were able to grow while others remained unable to grow. Review the data attached to order the biosynthetic pathway by both enzymatic step and by intermediate biomolecule. Label the step impacted by each of the mutant cell lines.the following is a coenzyme or cofactor involved in enzymatic reaction. identify the biochemical role that S-adenosylmethionine plays within a biochemical tranformation.
- You are required to isolate, purify and verify the purity of an enzyme from cytosol of a plant species for industrial use. Briefly describe how the desired enzyme can be obtained for the intended purpose stating the techniques involved. (MW of enzyme = 60 kbp)Compounds I, II, and III are in the following biochemical pathway: precursor compound I enzyme A enzyme B compound II ► compound III enzyme Mutation a inactivates enzyme A, mutation b inactivates enzyme B, and mutation c inactivates enzyme C. Mutants, each having one of these defects, were tested on minimal medium to which compound I, II, or III was added. Fill in the results expected of these tests by placing a plus sign (+) for growth or a minus sign (-) for no growth in the table below. Minimal medium to which is added Strain with mutation Compound I Compound II Compound IIIWhat are the results in the extraction of invertase from baker's yeast? (Lab purposes)
- What type of reactions would involve a ligase? neither anabolic nor catabolic anabolic exergonic catabolicXylanase is a class of hydrolyase enzymes that can break down hemicellulose into fermentable sugars. Xylanase is widely used in the pulp and paper industry for chlorine-free enzymatic bleaching of wood pulp. Besides that, xylanase is also applied in several industries like feed, pharmaceuticals, food and beverages. At the industrial scale, xylanases are mainly produced by microorganisms such as bacteria and fungi. 1. Solid-state fermentation and submerged fermentation are the two major techniques applied in the production of xylanase enzymes. Outline how the xylanase enzymes are produced using these two techniques. Identify the advantages and disadvantages of these two techniques. 2. Select a suitable microorganism and substrate that could be applied to produce xylanase enzymes economically at industrial scale via the submerged fermentation techniques with justifications.In the Avery experiment, mice were killed if they injected with S strain cells. Furthermore, incubation with extract from dead S strain cells could transform non pathogenic cells into pathogenic cells. This effect of S strain extract was eliminated if S strain extract is treated with what enzyme before incubation with non-pathogenic cells? protease DNAse RNAse Lipase
- The following are coenzymes or cofactors involved in enzymatic reactions. Identify the biochemical role that each plays within a biochemical transformation: Cofactor/Coenzyme Biochemical Role S-adenosylmethionine NADH NADPH FADH2 Biotin Pyridoxal Phosphate TetrahydrofolateWhich of the following is a substrate from primase?B-lactamase is an enzyme found in many antibiotic-resistant bacteria that hydrolyzes and inactivates antibiotics like penicillin and cephalosporin. The amount of antibiotic hydrolyzed in 1 minute in a 10-ml solution containing purified ß-lactamase was measured as a function of antibiotic concentration. The kinetics of hydrolysis was performed for two antibiotic substrates (A and B). Assume that the concentration of ß-lactamase was kept constant during the assay. 12 Initial Velocity (nanomole/min) 10 8 2 0 10 20 | 30 [Antibiotic] (µm) 40 50 Antibiotic A Antibiotic B a) Based on the enzyme description, what type of enzyme is ß-lactamase? Lyase Isomerase Ligase Hydrolase Oxidoreductase Transferase b) Based on your answer in (a), what other reactant, in addition to the antibiotic substrate, needs to be in the active site of ß-lactamase for the hydrolysis reaction to proceed? c) From the reaction curves above, what is the approximate value of Vmax for the enzyme reaction? (Do not forget the…