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BIOL 1F90 Lecture Notes - Lecture 10: Endoplasmic Reticulum, Golgi Apparatus, Nuclear Pore

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School
Brock University
Department
Biological Sciences
Course
BIOL 1F90
Professor
Linda Stillabower

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Document Summary

If the activation energy is large it means the reaction will take place very slowly. A substance that speeds up the rate of a chemical reaction by lowering the activation energy for the reason is not consumed in the reaction. A biological macromolecule that catalyzes or speeds up chemical reactions in biological systems. Enzyme activity is affect by temperature and ph. The site on an enzyme where the substrate binds where the chemical reaction that is catalyzed by the enzyme takes place. A reactant that interacts with the enzyme in an enzyme catalyzed reaction. The combined structure of an enzyme with a substrate that is bound to the enzyme s active site induced fit that end up close to certain chemical bonds on substrate . Depending on the enzyme the process of changing the substrate may be different they may.

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Related Questions

28. Which of the following statements about enzymes is false?

An enzyme changes shape when it binds to a substrate.

Enzymes lower the activation energy.

Enzymes are highly specific.

An enzyme may orient substrates, induce strain, or temporarily add chemical groups.

Most enzymes are much smaller than their substrates.

29. What is a transition state?

The place where a substrate molecule binds to an enzyme

A reactant with high potential energy

The combination of a substrate and an enzyme

The state at which the bonds of reactants are unstable

The active site where reactants are oriented

39. Which of the following statements about enzymes is true?

Enzymes are proteins.

Enzymes have a specific amino acid sequence.

enzymes are highly specific.

Enzymes lower the energy barrier.

All of the above

45. The catalysis mechanism used by lysozyme to break down bacterial cell walls is

acid–base catalysis.

covalent catalysis.

metal cofactor redox catalysis.

induced strain.

unknown.

46. Competitive inhibitors of enzymes work by

fitting into the active site.

fitting into a site other than the active site.

altering the shape of the enzyme.

changing the enzyme into an inactive form.

increasing the activation energy of the enzyme-catalyzed reaction.

47. Nerve gases such as Sarin and malathion

block specific chemical transformations by inactivating specific enzymes.

have reversible effects on animals.

are proteins with a primary structure.

block the energy coupling cycle of ATP.

bond covalently to the active site of the enzyme.

48. How do competitive and noncompetitive enzyme inhibitors differ?

Competitive inhibitors bind to the active site, whereas noncompetitive inhibitors change the shape of the active site.

Competitive inhibitors have a higher energy of activation than noncompetitive inhibitors have.

They function at different pH values.

Noncompetitive enzyme inhibitors contain magnesium, whereas competitive inhibitors contain iron.

Noncompetitive enzyme inhibitors are reversible, whereas competitive inhibitors are irreversible.

Which of the following statements describe(s) the characteristics of an enzyme active site that result in highly specific substrate selectivity and highly specific catalytic ability? (Select all that apply.)

a. The active site is a highly specific three-dimensional cleft or pocket formed from different parts of the primary amino acid sequence.

b. The active site takes up only a small part of the total enzyme.

c. Amino acid side chains at the active site combine to create a microenvironment where the arrangement of atoms is uniquely matched to characteristics of only a single substrate species.

d. Mostly weak interactions—H-bonding, van der Waals interactions, and hydrophobic interactions—function to bind the substrate to the active site.

e. Some amino acids at the active site actively participate in making and breaking of bonds by lowering the activation energy of the overall reaction.