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AP- Biology - Enzymes

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Section 1

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active site

Front

1 / 41

Biology Science

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Last updated

6 years ago

Date created

Mar 14, 2020

Cards (41)

Section 1

(41 cards)

active site

Front

the location on the enzyme where the substrate binds and goes through a chemical reaction.

Back

Shape

Front

in Biology the prefix allo means "different" and stereos means "__________"

Back

Reversible Inhibition

Front

When an enzyme inhibitor binds is similar to the substate and non-covalently bind to the active site and there slows down the enzyme

Back

hydrophobic

Front

Changes in H+ ions (acidity) concentration can alter how _____________ some regions of protein are.

Back

exothermic reaction

Front

a chemical reaction where energy is given off, so that the products have less energy than the reactants.

Back

coenzyme

Front

A non protein organic molecule serving to modify the active site of an enzyme before the reaction is allowed to occur. Most vitamins function important metabolic reactions in this role.

Back

endothermic reaction

Front

a chemical reaction where energy is taken in, so that the products have more energy than the reactants.

Back

Heme

Front

Organic molecules with iron an iron cofactor (A Prosthetic Group) that are permanently bond to enzyme responsible Oxygen transport

Back

Inducing Strain

Front

The enzyme cause bonds in the substrate to stretch

Back

Side chain (R group)

Front

the part of the enzyme that can add H+ ions to or from substrate destabilizing covalent bonds

Back

activation energy

Front

Eₐ is the abbreviation used for the energy required to start a reaction.

Back

G

Front

An exergonic reaction releases free energy. The abbreviation for free energy is: Named after the American Scientist Josiah Gibbs

Back

Transition State

Front

The less stable state that occurs and is usually a high-energy state between reactants and products in a chemical reaction

Back

Noncompetitive inhibitor

Front

a chemical that binds to an enzyme but not in the active site. This chemical will change the shape of the enzyme (reversible)

Back

Metal

Front

__________ ions such as Copper, Zinc iron bind to certain enzymes to initiated chemical reactions.

Back

Catalyst

Front

______ an agent that speeds up a chemical reaction without itself being permanently altered

Back

product

Front

compounds produced by a chemical reaction.

Back

reactants

Front

compounds that enter into a chemical reaction

Back

Hydrogen

Front

The specificity and activity of an enzyme depends on it 3D structure and this in turn depends on ______________ bonds

Back

Substrate Concentration

Front

After looking at the shape of graph the enzyme activity of this enzymes is being regulated by what variable:

Back

Activator

Front

A non-covalent binding regulator that can cause an enzyme to change shape and expose and expose an otherwise unexposed active site in allosteric regulation

Back

chemical reaction

Front

A process that changes one set of chemicals into another set of chemicals.

Back

amylase

Front

Enzyme that can break the bonds of starch to form the carbohydrate monomer, glucose.

Back

induced fit hypothesis

Front

The active site of the enzyme is flexible and conforms to fit the substrate like a glove fits on a hand.

Back

Protein Kinases

Front

enzymes that reversibly activate or inactivate other proteins by adding phosphate groups to (phosphorylating) them

Back

Temperature

Front

After looking at the shape of graph the enzyme activity of this enzymes is being regulated by what variable:

Back

nuclease

Front

Enzyme that can break the bonds of nucleic acids to form monomer, nucleotides

Back

lipase

Front

Enzyme that can break the bonds of lipids to form the monomer, fatty acids.

Back

Denature

Front

Characteristic of proteins; a change in shape that stops the protein from functioning.

Back

sucrase

Front

An enzyme that catalyzes the hydrolysis of sucrose into glucose and fructose

Back

Competitive inhibition

Front

substance that resembles the normal substrate competes with the substrate for the active site

Back

Substrate orientation

Front

When Enzyme bring together specific atoms into a correct position that are otherwise rotating and tumbling so that bonds can form

Back

Irreversible Inhibition

Front

When an enzyme inhibitor that covalently binds to the amino acid side chain at the active site of an enzyme it is called _______________

Back

Allosteric

Front

__________ regulation of enzyme occurs when a molecule binds to an enzyme changing the protein's shape

Back

enzyme

Front

biological catalysts usually globular that speed up the rate of chemical reactions

Back

pH

Front

After looking at the graph the enzyme activity of the the three different enzymes is being regulated by what variable

Back

Catalase

Front

an enzyme found in most aerobic organisms that breaks down H2O2 to water and oxygen

Back

protease

Front

Enzyme that can break the polypeptide bonds of proteins to form the monomer, amino acids.

Back

substrate

Front

the substance an enzyme catalyzes, changes.

Back

lock and key hypothesis

Front

The substrate fits the active site of the enzyme like a key fits in a lock. There is no change to the shape of the enzyme or substrate.

Back

activated complex

Front

the structure that is made up of the substrate bonded to the active site of the enzyme.

Back