Discuss factors affecting enzymatic reaction rates and explain enzyme kinetics.
Zero-order and first-order kinetics.
They are biological catalysts that speed up reactions.
Into six major classes.
In all body tissues, frequently appearing in serum following cellular injury.
A small organic molecule that serves as a cofactor in conjugated enzymes.
The nonprotein part of a conjugated enzyme.
The biochemically active conjugated enzyme produced from an apoenzyme and a cofactor.
An enzyme that consists of a protein and a non-protein component.
The enzyme acts on a particular type of chemical bond, regardless of the rest of the molecular structure.
The enzyme acts on a particular stereoisomer.
No, they are not consumed but help the reaction occur more rapidly.
-ase.
The enzyme will catalyze only one reaction, making it the most restrictive form of specificity.
No, it is not common.
Enzymes: Classifications.
German chemist Emil Fischer in 1894.
They catalyze reactions by lowering the activation energy level.
E represents the enzyme.
An enzyme that consists only of protein.
Using a system that provides information about their function, the type of reaction catalyzed, and the substrate identity.
Globular proteins.
The Lock and Key Model.
An enzyme that has a nonprotein part (cofactor) in addition to a protein part (apoenzyme).
ES.
The extent to which an enzyme’s activity is restricted to a specific substrate, a specific group of substrates, a specific type of chemical bond, or a specific type of chemical reaction.
The changes in the shape of a glove when a hand is inserted.
The enzyme has a specific shape that directly correlates to the shape of the substrate.
P represents the product.
Daniel Koshland.
The type of reaction catalyzed by the enzyme.
It must maintain a specific shape required for the reaction.
E + S → ES → E + P, where E is the enzyme, S is the substrate, ES is the enzyme-substrate complex, and P is the product.
Simple enzymes and conjugated enzymes.
The enzyme acts only on molecules with a specific functional group, such as hydroxyl (-OH), amino (-NH2), or phosphate groups (PO4).
The enzyme modifies the shape of the active site to accommodate the substrate.
Catalase.
The identity of the substrate.
Different levels of selectivity/specificity for substrates.
100 million times faster.
Enzymes are larger than non-biochemical catalysts.
No, all enzymes are proteins but not all proteins are enzymes.
Only protein (amino acid chains).
Holoenzyme.
Nucleoproteins or Glycoproteins.
Entirely of amino acid chains.
Glucose oxidase, pyruvate carboxylase, or succinate dehydrogenase.
Simple enzymes and conjugated enzymes.
S represents the substrate.
Substances present in the cell.
Lipase, Amylase, Trypsin, or Helicase.
