Enzymes GapFill

Enzymes have specific tertiary structures that result in the formation of an active site, a region where  an activatora basea producta substrate can bind to form  a substrate-product complexa prosthetic groupan enzyme-substrate complexa membrane-bound enzyme. The first hypothesis for how this worked was called the lock and key hypothesis, but a model which better explains this transition state is the  hydrophilic-channelremodelled-fitinduced-fitpermanent-fit hypothesis.

Enzymes lower the  water potentialtemperatureactivation energypressure of reactions, which speeds up the rate when they are present. However, their effectiveness can be compromised; for example, if a  lownon-optimaldecreasingincreasing pH or temperature is used and they become  exhaustedgelatinousbrittledenatured, or if the  solvent or active siteenzyme or substratesubstrate or productproduct or solvent concentration is too low. They are also susceptible to competitive inhibitors. which block their  poressequence endssecondary structuresactive sites, and non-competitive inhibitors, which change their overall shape.

An example of an intracellular enzyme is  helicasecatalasetrypsinpepsin, which breaks down hydrogen peroxide into water and oxygen. Amylase is an extracellular enzyme because it digests  starchfatty acidsglucosetriglycerides outside of cells. It requires  a coenzymean activatora by-producta cofactor to function properly; in this case, a  H⁺Cl⁻K⁺Ca²⁺ ion. Other enzymes may be permanently bound to a non-protein group which helps it function, called  a coenzymea by-producta prosthetic groupa precursor.