INTRODUCTION TO ENZYMOLOGY
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Study of enzymes 1. Activity of enzymes 2. Chemical reactions it catalyzes 3. Clinical use
enzymology
Increases the speed of reaction
Protein catalysts
AKA excess energy
Activation Energy
The molecule upon which an enzyme acts
substrate
Specific biologic proteins that catalyze biochemical reactions
enzymes
Often water-free cavity. Region of an enzyme where substrate molecules bind and undergo chemical reaction
active site
changing the shape of the enzyme or confirmation
Allosteric Site
impairs activity of the enzyme
Allosteric inhibitor
enhances activity of the enzyme
Allosteric activator
Results when an enzyme is subject to posttranslational modification
Isoform
Isoform of enzymes. Enzyme existing in different forms within the same individual but the same action
Isoenzyme
Organic cofactor such as nicotinamide adenine dinucleotide
Coenzyme
Inorganic cofactor like chloride ion, magnesium ion
Activator
Nonprotein molecule that may be necessary for enzyme activity
Cofactor
coenzyme that is bound tightly to the enzyme
Prosthetic group
Ability of an enzyme to choose exact substrate from a group of similar chemical molecules
Enzyme Specificity
• Enzymes may recognize and catalyze • A single substrate • A group of similar substrates • A particular type of blood
Enzyme Specificity
AKA Zymogen Inactive form or precursor of enzyme
proenzyme
Oxidation and reduction
Oxidoreductase
– removal of H ion
Oxidation
– accept H ion
Reduction
Addition of water to a bond resulting in bond breakage
Hydrolases
Transfer of functional groups other than hydrogen from one substrate to another
Transferases
Catalyze the joining of two large molecules by forming a new chemical bond
Ligases