Serine 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 sure

Serine 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 sure

Biochemistry

6th Edition

ISBN:9781305577206

Author:Reginald H. Garrett, Charles M. Grisham

Publisher:Reginald H. Garrett, Charles M. Grisham

Chapter31: Completing The Protein Life Cycle: Folding, Processing, And Degradation

Section: Chapter Questions

Problem 15P

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Shown below is a substrate for a Trypsin. Draw the mechanism for this serine protease using the artificial substrate. Be sure to draw the catalytic triad, and show the role of the oxyanion hole. Draw the complete structure of every intermediate and product and PUSH ARROWS!!!!! Do not abbreviate structures using R and R' H₂N _N_CH. сно CH₂ CH₂ CH₂ NH d=19H₂ NH₂ O CH- H₂C HN O CH
Please select appropriate word in each bracket Many anti-cancer drugs affect nucleotide metabolism and inhibit DNA synthesis. For example, a widely used anti-cancer agent, 5-fluorouracil, is a pyrimidine analog that is incorporated into nucleotide form and affects DNA synthesis by inhibiting the activity of [ Select ] ["thymidine kinase", "ribunucleotide reductase"] , the enzyme required to synthesize [ Select ] ["dTMP", "dUMP"] . This inhibition of DNA replication affects both cancer and normal cells, and hence there are serious side effects of these agents including [ Select ] ["immune system suppression", "hyperallergenic reaction"] and damage to the [ Select ] ["lining of the GI tract", "connective tissue of cartilage"] . Methotrexate, was the first drug to actually cure a cancer, choriocarcinoma, in 1958, and serves to block the activity of [ Select ] ["dihydrofolate reductase", "serine hydroxymethyl-transferase"] , another enzyme required for the synthesis of dTMP.
Chemical labeling of chymotrypsin by the compound tosylphenylalanine chloromethyl ketone (TPCK) modifies the His 57 in the enzyme's active site. The structure of this derivative is shown below. TPCK inactivates the enzyme because the bulky addition prevents it from cleaving nearby covalent bonds. HCI + CH, C-O Chymotrypsin-His 57 TPCK Modified enzyme True O False
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!
A chain NH3 NH3 B chain Gly Phe 2. The protein pictured below is bovine insulin. Determine the number and the size of the fragments that would be generated upon treatment with the following: İle Val Val Asn Gln Gln 5 Ġln 5 His look for the cleavage points (a) without DTT and (b) with DTT. Cys Leu Cys S-S Cys Without DTT With DTT Ala Ģly Ser Ser Trypsin 10 Val 10 His Cys Leu Chymotrypsin Ser Val Leu Glu BrCN Tyr Ala 15 Gln 15 Leu Leu Тyr Ġlu Leu Ásn Val Тyr Cys 20 Çys 20 Gly Asn Glu Arg Reagent (source) Trypsin (bovine pancrease) Chymotrypsin (bovine pancrease) Staphylococcus V8 protease Pepsin (porcine pancrease) Cyanogen bromide (chemical)(CnBr) Specificity Lys, Arg (C) Phe, Trp, Tyr (C) Glu, Asp (C) Phe, Trp, Tyr (N) Met (C) Gly Phe 25 Phe Тyr Thr Pro Lys 30 Ála
what 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.
Plz answer correctly do not copy. Question- Arsinate binds to reduced thio groups such as those found in cystiene residues in proteins, lipoate or glutathione. The resulting inhibition leads to central nervous system pathologies. The binding of arsinate to the dihydrolipoyl groups inhibits which of the following enzyme(s)? succinate dehydrogenase malate dehydrogenase pyruvate dehydrogenase complex branched-chain amino acid dehydrogenase complex isocitrate dehydrogenase alpha-ketoglutarate dehydrogenase complex
Structures of L-Cysteine from highly protonated to depronated form. Note Structure A as themost protonated form. Based on the table, 1. Show charges and pKa summary then calculate for pI value.
Need help Sesamin is one of the major lignans found in sesame oil. Sesamin-metabolic pathways remain uncharacterized at both the enzyme and gene levels. However, one microorganism showed significant sesamin-degrading activity and was identified as Sinomonas sp. no. 22. A sesamin- metabolizing enzyme named SesA was purified from this strain and characterized. Explain how sesamin methylene transferase was identified and characterized and explain the mechanism. Based on your knowledge, what other assays could be run to characterize this enzyme?
8 of 15 An enzvme has an all-important histidine residue in its active site such that substitution with an other amino acid would result to the loss of catalytic activity. What are the possible mechanisms by which this histidine residue may facilitate catalysis? I. Acting as proton acceptor. II. Forming of covalent bond with the substrate via an ester bond. III. Serve as stabilizer of electrophilic substrate because of its nucleophilic character. Select the correct response: land II Il and III land IlI I. Il, and III
Question #1: Choanoflagelletes are a unicellular ancestor to animals. One observation to support this hypothesis is the appearance of adhesion molecules that are key to the development of multiceullarity. Bulk transport Gap junctions Animals. Adhesion, cell signaling Single-celled :} Insects, mammals, and other animals with bilateral symmetry (~10,000,000) Jellyfish and their relatives (10,000) } Sponges (10,000) Choanoflagellates (150) Despite their simple unicellular lifestyle they express adhesion molecules including cadherins and lectins (King et al., 2003) but don't seem to have molecules that are typically found in the extracellular matrix such as integrins or laminins (Williams et al., 2014). Design a microscopy experiment to test the assertion that choanoflagellates have (some) adhesion molecules and those molecules play a similar role in a closely related animal like sponges.
Lysozyme is an antibacterial enzyme found in animals. Residues Asp 101 and Arg 114 are required for efficient catalysis, although they are located at some distance from the active site Glu 35 and Asp 52. Substituting Ala for either Asp 101 or Arg 114 does not significantly alter the enzyme's tertiary structure, but significantly reduces its catalytic activity. Explain.