Topic 3

a coenzyme

an allosteric inhibitor

a competitive inhibitor

the substrate

All increase when temperature increases.

All are produced by ionic bonding.

All are properties related to hydrogen bonding.

All have to do with nonpolar covalent bonds.

C and D only

The temperature at which it is operating

The optimum pH of the enzymes

The concentration of the substrate

The structure of the enzyme molecule

ionic bonds

nonpolar covalent bonds

polar covalent bonds

hydrogen bonds

It forms part of the structure of amino acids.

It forms part of the structure of fatty acids.

It forms part of the structure of ribose.

It forms part of the structure of nucleotides/ DNA

As channels for passive transport

As enzymes

As energy storage

As components of the animal cell wall

A. Glycogen

B. Starch

C. Fructose

D. A and B only

Dehydration reactions assemble polymers, and hydrolysis breaks down polymers.

Hydrolysis only occurs in the urinary system, and dehydration reactions only occur in the digestive tract.

Dehydration reactions can occur only after hydrolysis.

Hydrolysis creates monomers, and dehydration reactions break down polymers.

metabolic inhibition

feedback inhibition.

allosteric inhibition.

noncooperative inhibition.

Hormone

Energy Storage

Transport

Structure

bringing glucose and fructose together to form sucrose.

the release of water from sucrose as the bond between glucose and fructose is broken.

breaking the bond between glucose and fructose and forming new bonds from the atoms of water.

production of water from the sugar as bonds are broken between the glucose monomers.

utilization of water as a covalent bond is formed between glucose and fructose to form sucrase.

High specific heat

Transparency

Versatility as a solvent

It has its greatest density at 4°C

Hydrogen bonds between water molecules

Hydrogen bonds between hydrogen and oxygen within water molecules

Cohesion between water molecules and the container in which the water is boiled

Covalent bonds between hydrogen and oxygen within water molecules

Enzymes decrease the energy change of a reaction.

Enzymes increase the rate of a reaction.

Enzymes change the direction of chemical reactions.

Enzymes are permanently altered by the reactions they catalyze.

As a component in nucleic acids

As a component of lipids

As a component of carbohydrates

As a component of proteins

I only

II and III only

I and II only

I, II, III only

Active sites on enzymes are specific to a single substrate.

The shape of the active site can be changed by the binding of an allosteric inhibitor.

The binding of the substrate changes the shape of the active site slightly.

Competitive inhibitors can change the shape of enzymes.

Substrate concentration

A competitive inhibitor

High temperature

Low salt concentration.

The substrate molecules collide more frequently with the active site

There are more active sites to catalyse the reaction.

The substrate molecules are moving faster.

There are more substrate molecules to catalyse the reaction.

The part of an enzyme that binds only to the product molecules.

The sequence of amino acids responsible for the catalytic activity of enzymes

The sequence of amino acids responsible for the structure of an enzyme.

. The specific area responsible for the activity of all proteins.

entropy.

activation energy.

endothermic level.

heat content.

Ribose

Glycogen

Amylase

Glycerol

Cellulose

Carbonate

Water

Pyruvate

I and II only

II and III only

I and III only

I, II, and III

They are both polymers of glucose.

They are both used for energy storage in plants.

They can both be digested by humans.

they are both structural components of the plant cell wall.

Energy Storage

Enzymatic activity

Oxygen uptake

thermal insulation

functional groups.

vital forces interacting with matter.

carbon compound

water and its interaction with other kinds of molecules.

Carbon

Hydrogen

Nitrogen

Sulphur