Protease enzymes cleave proteins by hydrolyzing peptidebonds. The strategy for each type of metalloprotease beginswith generating a nucleophile that attacks the peptide bondthat attacks the peptide carbonyl group.O Macmillan LearningOn the basis of the information provided in the figure, showthe next step in the mechanism for peptide-bond cleavageby a metalloprotease.MetalloproteasesHR₁HNZnEnz2+R₂Draw curved arrows on the pre-drawn structures toshow the metalloprotease mechanism. If you need toreset the structures, click More followed byReset Drawing.Select Draw Templates Groups MoreB - HEnzHHсR1|: HNO|Zn2+BR2N ZnErase

Protein digestion and regulation are greatly aided by proteases, sometimes referred to as peptidases…

Answered: Protease enzymes cleave proteins by…

Biology: The Dynamic Science (MindTap Course List)

4th Edition

ISBN:9781305389892

Author:Peter J. Russell, Paul E. Hertz, Beverly McMillan

Publisher:Peter J. Russell, Paul E. Hertz, Beverly McMillan

Chapter4: Cells

Section: Chapter Questions

Problem 1ITD

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(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?
The glycosaminoglycan polysaccharide chainsthat are linked to specific core proteins to form the pro-teoglycan components of the extracellular space arehighly negatively charged. How do you suppose thesenegatively charged polysaccharide chains help to estab-lish a hydrated gel-like environment around the cell? Howwould the properties of these molecules differ if the poly-saccharide chains were uncharged?
. The following diagram shows the biosynthesis of B12 coenzymes, starting with the vitamin. DMB is dimethylbenzimidazole. (a) What one additional substrate or cofactor is required by enzyme B? (b) Genetic deficiency in animals of enzyme C would result in exces- sive urinary excretion of what compound?
complete the following mechanism showing the cleavge of the peptide bond for the following cysteine protease reaction. you only need a catalytic dyad for cystein proteases because the pKa of cysteine is low enough (8) and close enough to the pH of 7.4 that is can easily be deprotonated by histidine.
If the substrate for an enzyme catalyzed reaction contained a negative charge, which of the following amino acids would most likely be present in the active site to provide electrostatic destabilization of the ES complex? Leu Val O Asp O LYS QUESTION 15 What is the function of the histidine in the diagram of the mechanism at right with the substrate, a phenylalanine residue? (n) His Asp Nucleophilic affack by water stabilization of a metal ion covalent catalysis electrostatic attraction of the substrate O acid base catalysis 789 Mustly cloudy Click Save and Submit to save and submit. Click Save All Ansuwers to save all answers. here to search
Proteoglycan aggregates in tissues form hydrated, viscousgels. Can you think of any obvious mechanical reason whytheir capacity to form gels is important to cell function?[Hint: Liquid water is virtually incompressible.]
When performing his experiments on protein refolding, Christian Anfinsen obtained a quite different result when reduced ribonuclease was reoxidized while it was still in 8 M urea and the preparation was then dialyzed to remove the urea. Ribonuclease reoxidized in this way had only 1% of the enzymatic activity of the native protein. Why were the outcomes so different when reduced ribonuclease was reoxidized in the presence and absence of urea?
The diagram below shows the substrate binding cleft for a protease, providing the substrate structure, and indicating the residues (using one-letter code) that line the four specificity pockets. 1 M F H₂N K R IZ 2 3 P F S W оо E 4 The protease is known to cleave the amide linkage between W and E residues for substrates containing the WEFD sequence. Using 3-letter code with amino acids linked by a "dash" (ex. GLY-ALA), the N-terminal product is A and the C-terminal product is A
Identify each reaction catalyzed by (a) a nucdeotidase; (b) a phosphorylase; (c) a phosphoribosyltransferase. GMP A D E Guanine Guanosine F
The amln0 acid histldine ls usually found in actlve sltes 0f enzymes. What structural feature does the R group of hlstidine have that may be important for the activity of enzymes? Explain
if the reaction pH drops significantly (pH=2 for example), how would reaction catalyzed be serine proteases be affected? why? (assumin that the rest of the protein structure remain intact)
Consider a hexapeptide of the sequence thr asn glu trp lys gln. After complete hydrolysis, which amino acid would elute first from a cation exchange column at pH 7? O Asn O GIn Thr Glu O Trp O Lys

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