82.6.3 Part CElastase is closely related to chymotrypsin. Suggest two kinds of amino acid residues you might expectto find in or near the active site.Check all that apply.prolineserinevalinehistidinealanineSubmit Previous Answers Request AnswerX Incorrect; Try Again

there are four classes of biological macromolecules: nucleic acids, proteins, lipids and…

Answered: Part C Elastase is closely related to…

Biochemistry

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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

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Answer the following questions based on the structure of the following peptide and the information in the attached table of enzyme activities. M-F-V-W-E-Q-A-P-S-P-L Subjecting this peptide to trypsin would result in OA Met-Phe-Val-Trp-Glu-Gin-Ala-Pro-Ser-Pro-Lys Met-Phe-Val-Trp-Glu-Gin-Ala-Pro-Ser-Pro-Leu OB. Met-Phe-Val-Trp-Glu-Gin-Arg-Pro-Ser-Pro-Leu OC. D. Met-Phe-Val-Trp-Glu-Gin-Arg and Pro-Ser-Pro-Lys O E. Met-Phe-Val-Trp and Glu-Gin-Arg-Pro-Ser-Pro-Leu
the following is a coenzyme or cofactor involved in enzymatic reaction. identify the biochemical role that S-adenosylmethionine plays within a biochemical tranformation.
What step ends the first-half of the chymotrypsin mechanism? Attack of water on the acyl-enzyme intermediate. Selected Collapse of the first tetrahedral intermediate, releasing of the C-terminal peptide fragment and formation of the acyl-enzyme intermediate. Deprotonation of serine by the histidine. Collapse of the second tetrahedral intermediate leading to the final products. REVIEW QUESTION 1/1 CONTINUE MacBook Pro https://virginiacommonwealth.instructure.com/courses/42082/assignments/271397 esc OT
In 2-3 paragraphs (must be typed) explain: Discuss the regulation of cholesterol synthesis.
Match the enzymatic activity with the proper description within the ubiquitin-proteasome pathway. Drag and drop options on the right-hand side and submit. For keyboard navigation... SHOW MORE ✓ E1 E2 E3 Proteasome = ||| = ||| = ||| Degradation Ubiquitin-activating enzymes Ubiquitin-conjugating enzymes. Ubiquitin ligases
+ edu.au/courses/26618/quizzes/67364/take The image below shows the urea cycle. Based on the information in the image, which of the following is the most effective way of reducing the production of urea? CNH, Fumarate Arginine H₂O Arginase NH3+ C=N Arginino- succinate AMP + PP₁ NH₂ Arginino- succinase UREA CYCLE Urea ATP Argininosuccinate synthetase Ornithine H₂N H₂N 2 Citrulline Rate- limiting Ornithine 1. Carbamoyl phosphate synthase 1 N-acetyl glutamate H+ADP P₁ NH3 HCO3 ATP Carbamoyl Phosph. NH₂C-PO4 Ornithine 2. Citrulline formation P Citrulline C-NH₂ transcarbamoylase Aspartate NH₂ CYTOSOL MITOCHONDRIAL MATRIX https://canvas.uts.edu.au/assessment questions/356957/files/1562677/download? verifier=gRMPoy7VCgDrvn6QNfkZxDSsbLUwP1gRxFB3dLPj
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From the oligopeptide below, write completely the amino acids and/or peptide fragments that resulted from the reaction of elastase. The amino acids and residues should be represented by the three-letter abbreviation.
H CH₂ H₂C HC-CH3 CH₂ H H₂C (S) H₂C H CH₂ CH₂ CH₂ NH O C NH NH₂ a) Which of the following statements about this peptide are correct? Group of answer choices Treatment of this peptide with trypsin generates two products. This peptide is a substrate for carboxypeptidase A Treatment of this peptide with cyanogen bromide generates a pentapeptide and a tripeptide. Treatment of this peptide with chymotrypsin generates three products. Treatment of this peptide with elastase generates 2 products. None of the above statements are correct. b) What is the sequence of this peptide using one letter abbreviations? c) What is the pH which would correspond to the ionization of the peptide as drawn above? 1, 5, 7, 10, 14
lete this portion until 9.22, if so- just submit the first page of this worksheet ) Refer to the figure shown. Suppose that three critical amino acids in the active site of a specific enzyme are lysine, histidine, and arginine. HYDROPHOBIC AMINO ACIDS HYDROPHILIC AMINO ACIDS *H,N- CH -CO "H,N-CH- COO H,N-CH-COO Polar Which of the following characteristics would you predict the substrate to possess in order CH, CH "H,N-CH-COO H,N- CH - C0 CH, HC CH, CH, CH, CH Alanine (Ala. A) CH Valine (Val, V) CH THN C-NH, Leucine (Leu, L) Asparagine (Asn, N) Glutamine (Gin, Q) to bind the active site of this "H,N- CH -COO "H,N-CH-COO "H,N-CH-COO CH "H,N-CH-COO "H,N-CH-CO enzyme? CH CH- CH CH2 H C- CH, CH OH OH S-CH A. hydrophilic, with a positive charge Serine Threonine Isoleucine (le, I) Methianine (Met, M) Phenylalanine (Phe, F) (Ser, S) (Thr, T) Basic "H,N-CH-coO* "H,N-CH-COO "H,N- CH-COO "H,N- CH-- C00 "H,N-CH–COO CH CH CH, CH, CH, B. hydrophilic, but uncharged CH CH, NH NH CH, "H;N CH, H -N-)-…
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Part C Elastase is closely related to chymotrypsin. Suggest two kinds of amino acid residues you might expect to find in or near the active site. Check all that apply. proline serine valine histidine alanine Submit Previous Answers Request Answer