the structures of chymotrypsin and other serine proteases revealed that the active sites of these enzymes shared a particular sterochemicalarrangement of residues crucial to their activity. This came to be known as the catalytic triad, as it consisted of the oponyomous serine (Ser)residue, along with a histidine (His) and an aspartate (Asp) residue. Which of the following would result in the greatest decrease in function of thecatalytic triad found in serine proteases?O Mutation to Ser, Cys, AspO Mutation to Ser, His, AspO Mutation to Cys, His, AspO Mutation to Ser, His, Glu

Chymotrypsin and trypsin are examples of serine proteases. Chymotrypsin cleaves the peptides of…

Answered: the structures of chymotrypsin and…

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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Similar questions

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.
In the case of normal RNase A, Anfisen found that oxidizing the Cys residues before slowly removing the urea gave a very different result than oxidizing the Cys after slowly removing the urea. When the urea was removed first, Anfisen recovered 100% of the catalytic activity. When the urea was removed after oxidation, only about 1% of the activity (1/105) was recovered. The conclusion was that 104 of every 105 molecules was misfolded, and therefore catalytically inactive. Let's say someone raises an objection to this interpretation, and says that perhaps, instead, something chemically happens to the active site of RNase A when it is oxidized before refolding, and that the ~1% activity measured represents the residual and greatly reduced enzyme activity of all of the molecules, and the number is just coincidently similar to 1/105. (In other words, instead of 104 completely inactive molecules for every 1 completely active molecule, all molecules are equally damaged, and only function at…
PFK-1 is actually a tetramer with four identical active sites that produced fructose 1,6-bisphosphate. There are also allosteric sites for citrate and ATP/ADP on each subunit as well which influence how well the active sites are binding substrates or producing product. The arginine at position 48 on each PFK-1 subunit normally forms a salt bridge with a negatively charged oxygen on phosphate in the catalytic interface of PFK-1. Speculate on how the R48C mutation might change this function.
Which of the following statements about ribozyme catalytic residues is INCORRECT? General acid catalysis requires the standarde nucleotide exchangeable proton acidities (represented by pKa values). Ribozymes work by lowering the AG‡ through transition state stabilization without changing the overall AG of the reaction. Some ribozymes cleave phosphodiester bonds, and like proteases, can be autocatalytic. There are fewer known classes of mammalian ribozymes than mammalian enzyles.
From the complete oxidation of glucose (glucose → 6CO2), how many total nucleotide triphosphates are yielded (be sure to deduct payback) as part of substrate level phosphorylation?
“Caspase” describes the catalytic activity of this enzyme. What amino acyl residue participates in the catalytic mechanism? What substrate motif does caspase-8 recognize?
Hepatocellular carcinoma (HCC) is among the leading causes of cancer death worldwide. Studies of gene expression in HCC cells demonstrated that the enzyme ornithine aminotransferase (OAT) is upregulated in these cells. Ornithine (structure to the right) is both an intermediate in the urea cycle as well as a precursor for the synthesis of the nonessential amino acid proline. Unlike many aminotransferases, OAT acts on the side chain amine of ornithine rather than the alpha-amino 3. group. If OAT takes ornithine and alpha-ketoglutarate as (a) substrates, draw the structures of the products released after catalysis. (b) What cofactor does OAT use and how is it linked to the enzyme? Devise a strategy to alleviate HCC based on OAT and describe the specific steps required (c) to accomplish this. What is a major challenge in this approach? What pre-clinical effects would you want to demonstrate before attempting to treat patients?
Enzymes are stereochemically specific; that is, they oftenconvert only one stereoisomeric form of substrate intoproduct. Why is such specificity inherent in theirstructure?
In the salvage of purines, hypoxanthine-guanine phosphoribosyltransferase (HGPRT) is responsible for which of the following processes? Conversion of hypoxanthine to xanthine Conversion of adenine to adenosine monophosphate (AMP) Conversion of guanine to guanosine monophosphate (GMP) Conversion of inosine monophosphate to inosine
The hexokinases are a class of enzymes that catalyze the ATP-dependent phosphorylation of hexoses (sugars with six carbons). The hexokinases will bind only D-hexose sugars and not their L-counterparts. In general terms, describe the features of enzyme structure that make this specificity possible.
Construct the mechanism of a serine-protease with a catalytic triad.
The M and H subunits of lactate dehydrogenase have very similar sizes and shapes but differ in amino acidcomposition. If the only difference between the two were that theH subunit had a glutamic acid in a position where the M subunithad a serine, how would the five isozymes of LDH separate on electrophoresis using a gel at pH 8.6?

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