Enzyme Regulation - Allosteric Enzymes

Allosteric enzymes are multi-subunit proteins with one or more active site on each subunit.

Allosteric enzymes are multi-subunit proteins with one active site on their subunit.

Allosteric enzymes are proteins involved in making and breaking of covalent bonds.

Hyperbolic Curve

Sigmoidal Curve

Linear Regression

The binding of a substrate at one active site induces a conformational change in the protein that is conveyed to other active sites and altering their affinity for substrate molecules.

The binding of a substrate at one active site inhibits a conformational change in the protein.

The binding of a substrate at one active site induces a conformational change in the protein that is conveyed to other active sites and does not affect the affinity for substrate molecules.

Concerted Model

Ping-Pong Model

Michelis-Menten Model

Sequential Model

Synthesis of Pyrimidine – the formation of N-carbamoylaspartate.

Synthesis of Proteins - the formation of Peptide Bonds

Synthesis of Purines - the formation of Adenylate

Cytosine Triphosphate

Adenine Triphosphate

Cytosine Diphosphate

Adenosine Tri Phosphate, ATP - Allosteric Inhibitor

Adenosine Di Phosphate, ADP - Allosteric Activator

Adenosine Tri Phosphate, ATP - Allosteric Activator