They are catalysts and are not consumed in the reactions
They are proteins that act as a catalyst for biochemical reactions
The human body has 1000s of enzymes
They are the most effective catalysts known
Most enzymes are globular proteins
A few enzymes are now known to be ribonucleic acids (RNA)
They undergo all the reactions of proteins including denaturation
Enzyme activity
It is dramatically affected by alterations in pH
It is dramatically affected by temperature
It is dramatically affected by other protein denaturants
Simple enzyme
Composed only of protein (amino acid chains)
Conjugated enzyme
Has a nonprotein part in addition to a protein part
Apoenzyme
Protein part of a conjugated enzyme
Cofactor
Nonprotein part of a conjugated enzyme
Holoenzyme
The biochemically active conjugated enzyme
Cofactors
Small organic molecules or inorganic ions that are important for the chemically reactive enzymes
Co-enzymes/co-substrates
Organic molecule cofactors derived from dietary vitamins
Inorganic ion cofactors
Typical metal ion cofactors - Zn2+, Mg2+, Mn2+, and Fe2+
Nonmetallic ion cofactor - Cl-
Inorganic ion cofactors derived from dietary minerals
Substrate
The reactant in an enzyme-catalyzed reaction
Enzyme nomenclature
Most commonly named with reference to their function
Type of reaction catalyzed
Identity of the substrate
Suffix -ase
Identifies it as an enzyme
Suffix -in
Still found in the names of some digestive enzymes
Oxidase
Catalyzes an oxidation reaction
Hydrolase
Catalyzes a hydrolysis reaction
Six major classes of enzymes
Oxidoreductases
Transferases
Hydrolases
Lyases
Isomerases
Ligases
Oxidoreductase
Catalyzes an oxidation–reduction reaction
Transferase
Catalyzes the transfer of a functional group from one molecule to another
Transaminase
Catalyzes transfer of an amino group to a substrate
Kinase
Catalyzes transfer of a phosphate group from adenosine triphosphate (ATP) to a substrate
Hydrolase
Catalyzes a hydrolysis reaction involving the addition of a water molecule to a bond to cause bond breakage
Carbohydrases
Hydrolyze glycosidic bonds in oligo- and polysaccharides
Proteases
Effect the breaking of peptide linkages in proteins
Lipases
Effect the breaking of ester linkages in triacylglycerols
Lyase
Catalyzes the addition of a group to a double bond or the removal of a group to form a double bond in a manner that does not involve hydrolysis or oxidation
Dehydratase
Effects the removal of the components of water from a double bond
Hydratase
Effects the addition of the components of water to double bonds
Isomerase
Catalyzes the isomerization (rearrangement of atoms) reactions
Ligase
Catalyzes the formation of a bond between two molecules involving ATP hydrolysis
Active site
A relatively small part of an enzyme's structure that is actually involved in catalysis
Enzyme-substrate complex
Intermediate reaction species formed when substrate binds with the active site
Lock-and-key model
Enzyme has a pre-determined shape for the active site, only substrate of specific shape can bind
Induced fit model
Substrate contact with enzyme will change the shape of the active site to accommodate the substrate
Absolute specificity
An enzyme will catalyze a particular reaction for only one substrate
Stereochemical specificity
An enzyme can distinguish between stereoisomers
Group specificity
Involves structurally similar compounds that have the same functional groups
Linkage specificity
Involves a particular type of bond irrespective of the structural features in the vicinity of the bond
Higher temperature
Results in higher kinetic energy which causes an increase in number of reactant collisions, therefore there is higher enzyme activity
Optimum temperature
Temperature at which the rate of enzyme catalyzed reaction is maximum