BIOFOUND 3.2 Thermodynamics and Energy pt 2

substrate

the reactants of a chemical reaction

binding

the process in which substrates attach to enzymes

active site

the place where molecules bind to an enzyme

(1) altering the reaction pathway to one with lower activation energy (2) stabilizing the transition state

What are the two ways enzymes work together to make chemical reactions happen faster?

by binding them to a precise position, ensuring they are correctly positioned for the chemical reaction to occur quickly

How does the binding of substrates to an enzyme facilitate a chemical reaction?

ranges from no effect to complete dysfunction, potentially causing diseases or altering an organism's traits

what are the consequences of genetic changes in a proteins sequence?

it creates a specific active site where a substrate can bind and a reaction can occur

how does the 3D shape of protein allow enzymes to work?

conformational shift

changes in the shape of a protein

induced fit model

the biological theory of enzyme function

metabolic pathway

a series of several chemical reactions

metabolic chain

a type of metabolic pathway when the product of the final reaction is different from the initial substra

metabolic cycle

a type of metabolic pathway when the product of the final reaction recreates the initial substrate

activated enzyme

when a cell turns up or turns on to preform a chemical reaction more quickly

inhibited enzyme

when a cell turns down or turns off to preform a chemical reaction more slowly

by making small tweaks to the shape of the protein which change the speed that a chemical reaction is preformed

how does a cell alter the ability of its enzymes?

allosteric regulation

the change of an enzymes shape through the binding of an activator or inhibitor at a specific binding site

allosteric site of allosteric regulation

the second binding site where the regulatory molecule binds

regulatory molecule allosteric regulation

used by the allosteric site to bind a molecule

when a molecule binds to a site on an enzyme that is not the active site

how does allosteric activation occur?

when a molecule binds to an enzyme at a site other than the active site, causing the enzyme to change shape and become less effective at binding its substrate

how does allosteric inhibition occur?

usually inactive, and binding of an effector molecule changes its shape to either activate or inhibit its function

what does the protein do in default shapes in allosteric regulation?

it either becomes activated to perform its function or inhibited from doing so, depending on the effector molecule bound to it.

what does the protein do in shifted shapes in allosteric regulation?

phosphorylation

when a phosphate group is added to a protein, changing its activity or function

when a kinase enzyme adds a phosphate group to a protein, causing a change in its shape that activates its function

how does phosphorylation activation occur?

when a phosphate group is added to a protein, causing a shape change that reduces or stops its activity

how does phosphorylation inhibition occur?

proteins in their default shape are usually inactive or less active until a phosphate group is added to trigger a functional change

what do the proteins do in default shapes in phosphorylation?

proteins in shifted shapes are activated or inhibited to perform their function, depending on the addition or removal of phosphate groups

what do the proteins do in shifted shapes in phosphorylation?

when a molecule blocks the enzyme's active site, preventing the real substrate from binding

competitive inhibition

the regulatory molecule competes with the substrate for the enzyme's active site

how does the regulatory molecule act in competitive inhibition?

in allosteric regulation, the regulatory molecule binds to a separate site, changing the enzyme's shape to increase or decrease activity.

how does the regulatory molecule act in allosteric regulation?