With the exception of some RNAs that catalyze their own self-cleavage, all enzymes are proteins
Enzymes can increase the rate of a reaction by a factor of 10^9 to 10^20 over an uncatalyzed reaction
Some catalyze the reaction of only one compound
Others are stereoselective; for example, enzymes that catalyze the reactions of only L-amino acids
Others catalyze reactions of specific types of compounds or bonds; for example, trypsin catalyzes hydrolysis of peptide bonds formed by the carboxyl groups of Lys and Arg
Trypsin catalyzes the hydrolysis of peptide bonds formed by the carboxyl group of lysine and arginine
Classification of enzymes
Oxidoreductases: Oxidation-reduction reactions
Transferases: Group transfer reactions
Hydrolases: Hydrolysis reactions
Lyases: Addition of two groups to a C-C double bond, or removal of two groups to create a C-C double bond
Isomerases: Isomerization reactions
Ligases: The joining to two molecules
Oxidoreductase
Catalyzes oxidation-reduction reactions
Transferase
Catalyzes group transfer reactions
Hydrolase
Catalyzes hydrolysis reactions
Lyase
Catalyzes the addition of two groups to a C-C double bond, or removal of two groups to create a C-C double bond
Isomerase
Catalyzes isomerization reactions
Ligase
Catalyzes the joining of two molecules
Apoenzyme
The protein part of an enzyme
Cofactor
A nonprotein portion of an enzyme that is necessary for catalytic function; examples are metallic ions such as Zn2+ and Mg2+
Coenzyme
A nonprotein organic molecule, frequently a B vitamin, that acts as a cofactor
Substrate
The compound or compounds whose reaction an enzyme catalyzes
Active site
The specific portion of the enzyme to which a substrate binds during reaction
Activation
Any process that initiates or increases the activity of an enzyme
Inhibition
Any process that makes an active enzyme less active or inactive
Competitive inhibitor
A substance that binds to the active site of an enzyme thereby preventing binding of substrate
Noncompetitive inhibitor
Any substance that binds to a portion of the enzyme other than the active site and thereby inhibits the activity of the enzyme
Enzyme activity
A measure of how much a reaction rate is increased
Enzyme concentration increases
Reaction rate increases
Substrate concentration increases
Reaction rate increases
Temperature increases
Reaction rate increases
pH changes
Reaction rate changes
Lock-and-key model
The enzyme is a rigid three-dimensional body, and the enzyme surface contains the active site
Induced-fit model
The active site becomes modified to accommodate the substrate
Competitive inhibitor binds to active site
Substrate cannot bind
Noncompetitive inhibitor binds to site other than active site
Substrate can still bind but no catalysis occurs
Both the lock-and-key model and the induced-fit model emphasize the shape of the active site, but the chemistry of the active site is the most important
Five amino acids participate in the active site in more than 65% of the enzymes studied to date: His, Cys, Asp, Arg, Glu
Four of these five amino acids have either acidic or basic side chains; the fifth has a sulfhydryl group (-SH)
Feedback control
An enzyme-regulation process where the product of a series of enzyme-catalyzed reactions inhibits an earlier reaction in the sequence
Proenzyme (zymogen)
An inactive form of an enzyme that must have part of its polypeptide chain hydrolyzed and removed before it becomes active
Allosterism
Enzyme regulation based on an event occurring at a place other than the active site but that creates a change in the active site
Allosteric enzyme
An enzyme regulated by allosterism
Negative modulation
Inhibition of an allosteric enzyme
Positive modulation
Stimulation of an allosteric enzyme
Regulator
A substance that binds to an allosteric enzyme
Protein modification, especially phosphorylation/dephosphorylation, can affect enzyme activity
Isoenzyme (Isozymes)
An enzyme that occurs in multiple forms; each catalyzes the same reaction