The value of kcat for N-Ac-Phe-OC₂H5 is two-fold greater than that for the L-tryptophanyl analog and more than 10-fold greater than the value of kcat for the ester substrate N-Ac-Leu-OC2H5. Does this mean that N-Ac-Phe-OC2H5 exhibits greater specificity as a substrate than the other ester sub- strates? On what basis do you base your conclusion? Also, which kinetic parameters help to distin- guish between specificity (of substrate recognition) and affinity o0f a substrate when comparing a se- ries of substrates of an enzyme?
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- Draw the structure of the PTH derivative product you would obtain by Edman degradation of the following peptides: (a) I-L-P-F (b) D-T-S-G-AWrite out the structures for the cofactors involved in the following biochemical reactions: a) Methylation. b) Amino acid decarboxylation. c) A Claisen reaction. d) Ketoacid decarboxylation. e) Aldehyde reduction s ils otvteimaoomate nglaas bns vilanebl (d ienoiamlalblos tom orls ylianabl (o uencioiqeb of ezed aldstiua s jang2 (b adullb diiw aem (OatHer) nihshsw ( otsibammi dainiw (OatHer) 1aubong wan alobizobyrd moiboe ordt nadw owximAt 37 °C, the serine protease subtilisin has kcat = 50 s-1 and KM = 1.4 × 10-4 M. It is proposed that the N155 side chain contributes ahydrogen bond to the oxyanion hole of subtilisin. J. A. Wells and colleagues reported (1986, Phil. Trans. R. Soc. Lond. A 317:415–423) the following kinetic parameters for the N155T mutant of subtilisin: kcat = 0.02 s-1 and KM = 2 × 10-4 M.(a) Subtilisin is used in some laundry detergents to help remove protein-type stains. What unusual kind of stability does this suggest for subtilisin?(b) Subtilisin does have a problem in that it becomes inactivated by oxidation of a methionine close to the active site. Suggest a way to make abetter subtilisin.(c) Is the effect of the N155T mutation what you would expect for a residuethat makes up part of the oxyanion hole? How do the reported values ofkcat and KM support your answer?(d) Assuming that the T155 side chain cannot H-bond to the oxyanion intermediate, by how much (in kJ/mol) does N155 appear to stabilize…
- Determine the Primary amino acid sequence of an Octapeptide Composition · Tyr , Arg,Pro, Lys ,Lys ,Met ,Trp,Phe N terminal 1 2 3 4 5 6 7 8 C terminal 1) Treatment with an Edman reagent gives a PTH-AA that shows a Yellow color with Ninhydrin. 2) Trypsin digestion of the Octapeptide gives tetepeptide, dipeptide, free Arg ,free Trp. 3)CNBr = pentapeptide and tripeptide. 4) chymotrysin - tetapeptide and two dipeptiele. The tetrapeptide contains an amino acid with an OH group in the side chain.describe a detailed experimental procedure for the chemical synthesis of proteins with the α-ketoacid hydroxylamine (KAHA ligation), using (S)-5-oxaproline (Opr) as a key building block.The substitution of His 64 of carbonic anhydrase II with Ala results in a sharp decrease in the activity of the enzyme in HEPES buffer (molecular weight of HEPES = 238.3 g/mol). However, increasing concentrations of imidazole (molecular weight = 68.1 g/mol) restores the reaction rate close to that of the wild-type enzyme. Propose an explanation for these results.
- (i) Describe the mechanism of chymotrypsin in cleaving a peptide bond, highlighting the roles of the catalytice triad for the two phases of the catalytic reactions. Explain the significance of the oxyanion hole for the catalysis. (ii) All serine proteases contain the catalytic triad and these amino acids are positioned in the exact same conformation. Since this is true, why do trypsin and chymotrypsin have such different substrate specificity? What features of the enzyme allow for this situation?Chymotrypsin has the highest affinity for which of the following substrates: Table. The values of KM and kcat for some Enzymes and Substrates Enzyme Chymotrypsin Ки (М) 4.4 x 10-1 8.8 x 10-2 6.6 x 104 Kcat (S-1) 5.1 x 10-2 1.7 x 10-1 1.9 x 102 Substrate N-acetylglycine ethyl ester N-acetylvaline ethyl ester N-acetyltyrosine ethyl ester Catalase H2O2 2.5 x 10-2 1.0 x 107 Urease Urea 2.5 x 10-2 4.0 x 105 OA. N-acetylglycine ethyl ester OB. N-acetylvaline ethyl ester OC. N-acetyltyrosine ethyl ester D. Urea1. Please fully explain (use illustrate where appropriate) the Modes of Enzyme Catalysis exemplified by the serine protease: Chymotrypsin. In your answer discuss employing the illustration whenever possible: the overall reaction mechanism, stability of the reaction transition state, proximity and orientation effects, acid-base catalysis, and covalent catalysis. (c) (0) Ap Asp Toe His Asp 10 C-N bond cleavage HN Ho Ser Ger Binding of substi 196 Ser Gly alto video LBHB NH Sere HAR Proton donation by H (h) Fel of amino product yest OHN Hig Ser Ap (0) Formation of covalent (ES) Alp Me complex Serios
- #1 Specify the role each of the following amino acids play within the crystal structure and/or active site for Be as specific as possible, with pictures (and mechanistic arrows) as necessary. His11 Arg140 Glu89 Trp68 #2 Provide a step-wise mechanism for the reaction Bisphosphoglycerate mutase catalyzes, using the amino acids responsible for aiding in catalysis. You do not need to add surrounding amino acids that aid in substrate specificity. (drawn out)Glucosidase I catalyzes hydrolysis of specific glucosidase I is a synthetic trisaccharide, glucose-al-2- glucose-al-3-glucose-a-O(CH₂) #COOCH3. Kinetic measurements oligosaccharides containing glucose. obtained using this trisaccharide as substrate in the deoxynorjirimycin at concentrations of 50 μM (), 100 μM absence (x-x) and presence of the inhibitor 1- A) were used to prepare the (-), and 200 μM (4 Lineweaver-Burk plot below: b) Page 3 12) 7. a) V/V (nmol/hr)-1 1.S 1.0- 0.5 1/Trisaccharide (mM)-! Estimate the values for Vmax and KM for the trisaccharide substrate in the absence of the inhibitor. 0.0 -1.0 0.0 One substrate for 1.0 2.0 Determine whether inhibition by 1-deoxynorjirimycin is competitive, non-competitive or neither.The key reaction steps in the Edman degradation of polypeptides, which removes the N-terminal amino acid in the form of a "phenylthiohydantoin" (PTH-amino acid), are shown below. What is the expected outcome if the N-terminal amino acid is proline (Pro)? (The structure of proline is provided below for your reference.) NH-C00 NH CO0 phenyl isothiocyanate PITC NH CO0 NH CO0 peptide without the thiszolinone original Nterminal amino acid HE a PTH-amino acid Proline: HN HN. O Edman's reagent will not react with an N-terminal proline.