Asap possible solve all need solutions .no need explanation. Solve in 10mins Decide whether each of the following statements is true about ornithine carbamoyltransferase.It's a small molecule, with a molecular weight around 50molIt'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.truefalsetruefalsetruefalseOtruefalse

Ornithine carbamoyltransferase is an enzyme is important in the urea cycle. Urea cycle is a…

Answered: Decide whether each of the following…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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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
3CLpro is a cysteine protease, which are among the most common proteases in biochemistry, however they are a structurally diverse family of enzymes especially in the organization of the active site amino acids. A group of scientists have reported a potential drug molecule based on a binding study using circular dichroism. They report that the molecule binds to the active site. Can the experiment support the claims, why or why not? Which techniques might be used to support this claim?
Draw the catalytic triad of a serine protease at the first tetrahedryl intermediate stage. Your drawing should include the amino acids that make up the triad, any part of the substrate that should be present, and any other molecules that are present in the active site.
Why is the covalent intermediate of elastase stable at low pH? The catalytic histidine cannot act as general acid when protonated. O The catalytic histidine cannot act as a general base when protonated. The catalytic serine cannot form a covalent bond to substrate if the pH is below 7.4. O The catalytic serine cannot preferentially form a hydrogen bond with the catalytic histidine at acidic pH, causing these residues to shift out of their catalytically optimal positions.
The enzyme lysozyme hydrolyzes glycosidic bonds in peptidoglycan, an oligosaccharide found in bacterial cell walls. The active site of lysozyme contains two amino acid residues essential for catalysis: E35 and D52. Which of the following statements about lysozyme is true? More than one may apply The graph shows the pH-activity profile of lysozyme. 100 50 4. 6. 8. 10 pH Residue E35 exhibits general base catalysis O The pKa of E35 is approximately 4.3 O The pKa of D52 is approximately 4.5 O The optimal activity of lysozyme is approximately 5.2 Residue E35 exhibits covalent catalysis The pka of E35 is approximately 6.1 The pka of D52 is approximately 3.7 Activity (% of maximal)
Parts of the mechanism for lysozyme are shown below. The catalytic lysozyme residue side chains can be identified as being above and below the polysaccharide chain shown at point A. Complete the missing structures (points B and E) and curly arrows (points A, B, C, D and E) in the mechanism, as well as from the knowledge you have gained, label the catalytic amino acids at point A in your mechanism with their correct name and residue number. A OH R OH O-R H₂C- HO NHAC NHAC E R D OH B R C H RO H3C- ° H₂C- NHAC Y R OH NHAC R R
RuBP carboxylaseis by no means an idesl enzyme. Describe some of the problems with its active site and its substrate specificity. If we compare the amino acid sequences of this enzyme from many different species, they are almost identical. What is the significance of this uniformity?
Proteases are enzymes that cleave peptide bonds using general acid–base catalysis. General acid–base catalysis relies on a proton donor or acceptor other than water. Proteases rely on proton transfer to create strong nucleophiles from active-site amino acid residues. In the protease chymotrypsin, an active-site serine is a potent nucleophile. A nearby residue, His 57, interacts with serine to increase its reactivity. A schematic of chymotrypsin’s active site illustrates the active site Ser 195 and His 57 R groups. The Asp 102 residue helps position the His 57 residue via hydrogen bonding.
RuBP carboxylase is not an idel enzyme by any means. Describe some of the active site's and substrate specificity's issues. When the amino acid sequences of this enzyme from several species are compared, they are nearly similar. What importance does this homogeneity have?
Hydrolysis of a decapeptide yields the following amino acids. ala, asp, arg, his, leu, lyS, met, tyr The following fragments produced upon subjecting the decapeptide to various enzymatic and chemica hydrolysis Sanger's method: DNP-arg and nonapeptide Cyanogen bromide. met, leu-asp-his, and hexapeptide Trypsin: arg, ala-lys, and heptapeptide Chymotrypsin: tyr, arg-ala-lys-tyr, and pentapeptide Carboxypeptidase: his and nonapeptide Determine the amino acid sequence of the decapeptide: [ Select 1
Histidine is frequently used as a general acid or base in enzyme catalysis. Considering the pKa value of the side chain, suggest a reason why is this so?
b) Why might the compound shown below act as a transition state analog of phosphoglucose isomerase? A drawing of the normal transition state for this enzyme is needed. HO- OH T .N -OH -OH CH₂OPO₂²-

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