**Transcription for Educational Website:****Understanding Enzyme Functionality:**In most enzymes, the required active site amino acids consist of only a few residues. Why is the rest of the protein necessary for full enzyme function?- ○ To bind to the membrane through hydrophobic residues.- ○ To interact with other proteins so that the enzyme can be imported into the endoplasmic reticulum where enzymes are the most active.- ○ To provide the correct tertiary structure for the substrate binding site and for proper orientation of the catalytic residues.- ○ To provide protein targeting sequences so that the enzyme can be transported to the mitochondrial matrix where gluconeogenesis takes place.

Enzymes are proteins that function as biocatalysts and catalyse biochemical reactions.They have a…

Answered: In most enzymes, the required active…

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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Failure of anti-oxidant function results in the hydroxylation of an aromatic acid of Enzyme Z and its activation, so that it degrades protoporphyrin to porphyrin, an unstable product. When hit by light, this product further degrades to form a compound responsible for the lesions and excruciating pain the man suffers. The mutation also affected an amino acid at the N-terminal of Enzyme X. Sequencing of the first seven (7) amino acids at the N-terminal of the normal enzyme gave the following sequence: trp-arg-asp-leu-ser-gly-his When the cDNA was sequenced by the Sanger method utilizing ddCTP, the following products were obtained: Tetranucleotide Hexanucleotide Nonanucleotide Decanucleotide Dodenucleotide Octadecanucleotide Nonadecanucleotide 21-nucleotide The mutation involved the 19th bases of the template strand of the peptide. A comparison of the electrophoretic profile of the normal peptide (N) and mutant peptide (M) is shown below. The (+) electrode is situated at the bottom. pH…
A) Myth: Enzymes are specific for one substrate. Fact: Like most enzymes, alliinase can act on multiple different substrates. Explain why most enzymes can act on more than one substrate compound. (Refer to the “Alliin-like Substrates" panel in your answer.)
Failure of anti-oxidant function results in the hydroxylation of an aromatic acid of Enzyme Z and its activation, so that it degrades protoporphyrin to porphyrin, an unstable product. When hit by light, this product further degrades to form a compound responsible for the lesions and excruciating pain the man suffers. The mutation also affected an amino acid at the N-terminal of Enzyme X. Sequencing of the first seven (7) amino acids at the N-terminal of the normal enzyme gave the following sequence: trp-arg-asp-leu-ser-gly-his When the CDNA was sequenced by the Sanger method utilizing ddCTP, the following products were obtained: Tetranucleotide, Hexanucleotide, Nonanucleotide, Decanucleotide, Dodenucleotide, Octadecanucleotide, Nonadecanucleotide, 21-nucleotide What is the sequence of the bases in the mRNA coding for the peptide above? The mutation involved the 19 bases of the template strand of the peptide. A comparison of the electrophoretic profile of the normal peptided (N) and and…
The active site of an enzyme has a serine residue (shown below). Which of the following describes the substrate? H2N- CH- -OH OH polar active site, interacting atoms in substrate could be C-H Ononpolar active site, interacting atoms in substrate could be C-H polar active site, interacting atoms in substrate could be N-H nonpolar active site, interacting atoms in substrate could be N-H
Concerning enzymatic activity, a larger Km value indicates a/an: Select one: O lower affinity for its substrate O inhibitory process O larger enzyme O larger Vmax O greater affinity for the substrate Which is the least common type of chemical bond? Select one: O Hydrogen O Peptide O Covalent O lonic O Disulphide D-gluconic acid is: Select one: O an integral membrane protein O a codon O an oxidized sugar O phosphorylated O a large lipid molecule
The natural enzyme is recreated by mixing isolated regulatory and catalytic subunits of ATCase. What biological relevance does this observation have?
Changing which pairs of the amino acids is most likely to directly lead to the most severe problems with substrate (Blue) binding by the protein depicted by the red ribbon.
The trypsin enzyme is able to hydrolyze a peptide substate at the carboxyl side of an Arg or Lys residue. However, such a reaction can be also influenced by the amino acid residue that follows Arg or Lys. Given the Michaelis-Menton plots obtained for two substrates (substrate A: Ser-Val- Arg-Pro; substrate B: Ser-Val-Arg-Phe), the Km of the enzyme is higher for: 20 Substrate A Assume that these curves do not reach the same limit. 15 Substrate E 0.001 0.002 0.003 (Substrate) (molar) Inconclusive Substrate B Both Substrate A and B Intitial velocity (micromoles/literisecond)
what does the Hexa protein domain depict? (in relation with tay sachs disease)
. The allosterically regulated enzyme ATCase binds aspartic acid as a substrate and acylates the a-amino group. Succinate acts as a competitive inhibitor of ATCase because it binds the active site but can't be acylated. The dependence of vo on [aspartic acid] for ATCase is shown in panel (a) of the accompanying figure. Panel (b) shows the effect of increasing [succinate] on v, when [Asp] is held at a low concentration (see thick vertical arrow in panel (a)). Note that in panel (b), vo is not zero when [succinate] =0 (see thin horizontal arrow). Explain the shape of the curve in panel (b). Why does v, increase initially, before decreasing at higher [succinate]? Co0- COO CH2 CH, HC -NH, CH, COO COO Asp Succinate [Asp) [Succinate] [Asp] in experiment b (a) (b)
I have a fill in the blank question. "1) Heterophobic or Homotrophic effects= are changes in affinity due to substrate binding and cooperativity between different subunits. They give Allosteric rate curves their Sigmoid shape. 2) Hetero or Homotrophic effects=are changes in affinity due to binding of an effector to an Allosteric site. Allosteric sites are usually 3)located outside or inside the active site. Positive Allosteric effectors (activators) shift the rate curve 4) Left or Right, where Negative effectors shift it 5) right or left. Positive Allosteric effectors usually stabalize the 6)T or R state. Negative efftors usually satbalize the R state." Thank You!!!

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