Decide whether each of the following statements is true about ornithine carbamoyltransferase. It's a small molecule, with a molecular weight around 50 mol It's made by a ribosome out of amino acids. It's a substrate, and ornithine is its superstrate. It has no effect on the stability of ornithine, that is, it does not change the free energy of ornithine. O true false true false Otrue false O true false
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- Be sure to answer all parts. Give the amino acid sequence of an octapeptide that contains the amino acids Val, Met, Asp (2 equiv), Phe, Trp, Ile, Lys, and forms the following fragments when partially hydrolyzed with HCl: Ile-Asp-Phe, Lys-Met-Val-Trp, and Phe-Asp-Lys-Met. Trp Leu Phe Leu Val Lys Gly Tyr XSerine protease enzyme mutation To show differences in the effect of the nucleophilic attack of the carbonyl group (C=O) of peptide bond between the catalytic triad of serine, histidine and aspartic acid, and another catalytic triad contains alanine, histidine and aspartic acid Provide/ draw an example of catalytic mechanism with catalytic triad contains alanine, histidine and aspartic Please answer completely will give rating surelywhat is lactose intolerance ? describe the molecular life cycle for this disease. also describe how it occurs in a molecular level detailed mechanism. what causes this disease and how it develops ? provide detailed biochemical phenomena and life cycle for Lactose Intolerance condition.
- How do 3D model structure of transferase enzyme works? Give me a precise and accurate explanation. Thank you!Be sure to answer all parts. Give the amino acid sequence of an octapeptide that contains the amino acids Lys, Pro, Tyr, Ile (2 equiv) , Gln, Trp, Phe, and forms the following fragments when partially hydrolyzed with HCl: Lys–Ile-Phe-Pro, Phe-Pro-Gln-Tyr, and Trp-Ile-Lys.Chart is Given for you: Below is a chart of values for actual enzymes. Enzyme Km (M) kcat (1/s)Chymotrypsin 1.5 × 10^−2 0.14Pepsin 3.0 × 10^−4 0.5Tyrosyl-tRNA synthetase 9.0 × 10^−4 7.6Ribonuclease 7.9 × 10^−3 7.9 × 10^2Carbonic anhydrase 2.6 × 10^−2 4.0 × 10^5Fumarase 5.0 × 10^−6 8.0 × 10^2 Assume the enzyme concentration is equal across all samples (and is equal to 1). (Answer a and b only)a. Which enzyme will have the highest V0 at very high substrate concentrations? (1 M). Why? b. Which will have the highest V0 at very low substrate concentrations (5.0 × 10^−12). Why?
- The allosteric site 1). Draw a representation of an allosteric binding site of an enzyme. must bind an allosteric modifier that maintains three hydrophobic regions, a polar charged region and two regions of hydrogen bonding. You choose the order or organization of the characteristics in the allosteric site - label all regions. Details the allosteric site is composed of faces of two separate beta sheets and two separate alpha helices. You might decide that each beta sheet or each alpha helix contributes one amino acid R group to the allosteric site or you may decide that one of the beta sheets or one of the alpha helixes contributes two or more amino acid R groups to the allosteric organization. Your choice but please show R group structure in the allosteric site!I lea the - Oligopeptide 2 a. Give the three-letter and one-letter names of the amino acids in each oligopeptide starting from the amino terminal to the carboxyl terminal. Make sure that the amino acid names are arranged in CORRECT order for both oligopeptides. I b. After complete hydrolysis, which oligopeptide will yield more ATP molecules? How many NADH and FADH2 molecules will be theoretically produced? Show all relevant computations for each oligopeptide. Tabulate your answers to keep your answers organized. ( Oligopeptide Net ATP molecules Net NADH produced Net FADH2 produced produced Oligopeptide 1 Oligopeptide 2Unanswered Sa polysaccharides 1 Why are humans not able to digest cellulose? Select an answer and submit. For keyboard navigation, use the up/down arrow keys to select an answer. al Humans do not possess the enzyme necessary to hydrolyze the 1-4-B-glycoside linkages found in cellulose. Humans cannot digest glucose. Humans do not possess the enzyme necessary to unwind the helical shape of the cellulose molecule. P. Humans do not possess the enzyme necessary to oxidize OH groups in cellulose. Unanswered physical preperties 2
- Be sure to answer all parts. Give the amino acid sequence of an octapeptide that contains the amino acids Thr, Phe, Ile (2 equiv), Asp, Cys, Val, Leu, and forms the following fragments when partially hydrolyzed with HCl: Thr-Ile-Phe, Phe-Ile-Asp-Val, and Asp-Val-Cys-Leu.help fill in the word between brackets Serine proteases are an example of [nucleophilic/electrophilic/covalent/acid- base] catalysts because the catalytic triad [aspartate/serine/histidine] protonates the leaving group and abstracts a proton from water. Serine proteases are an example of [nucleophilic/electrophilic/covalent/acid-base] catalysts because the catalytic [aspartate/serine/histidine] is converted to an oxyanion to attack the peptide bond. Serine proteases are an example of [nucleophilic/electrophilic/covalent/acid-base] catalysts because an acyl-enzyme intermediate is formed during the catalytic cycle between part of the substrate and the catalytic [aspartate/serine/histidine].MULTIPLE CHOICE - Please answer properly QUESTION : Enzymes can be regulated in a many different ways. Covalent modification is one way. Here, the functional groups are attached to or removed from the enzyme. A phosphate group is an example of a functional group that can be added to an enzyme. Depending on the enzyme, addition of a phosphate group can either increase or decrease an enzyme's activity. Evaluate the following names and identify the general name of an enzyme that functions to add phosphate groups to its substrate? A. isomerase B. phosphatase C. kinase D. ligase