Aureolysin, along with V8, SspB, and ScpA, are all secreted a zymogens.
This means that they are secreted in an inactive conformation until the propeptide is removed in some manner.
Aureolysin, V8, and SspB constitute what is known as the staphylococcal proteolytic cascade.
All three of these proteases are secreted into the environment with the propeptide inhibiting their activation.
Aureolysin undergoes autocatalysis and the propeptide is degraded generating the mature form of the enzyme.
Mature aureolysin will then cleave the propeptide from V8, causing this protease to become active.
Finally V8 will cleave SspB propeptide and the cascade is now complete.
ScpA becomes mature by autocatalytic degradation of the propeptide, similar to that of aureolysin.

The active residues of aureolysin are of critical importance to its enzymatic function.
The active residue is a glutamate amino acid located at the 145th position of the protein.
Aureolysin, along with V8, SspB, and ScpA, are all secreted a zymogens. This means that they are secreted in an inactive conformation until the propeptide is removed in some manner. Aureolysin, V8, and SspB constitute what is known as the staphylococcal proteolytic cascade. All three of these proteases are secreted into the environment with the propeptide inhibiting their activation. Aureolysin undergoes autocatalysis and the propeptide is degraded generating the mature form of the enzyme. Mature aureolysin will then cleave the propeptide from V8, causing this protease to become active. Finally V8 will cleave SspB propeptide and the cascade is now complete. ScpA becomes mature by autocatalytic degradation of the propeptide, similar to that of aureolysin.
The active residues of aureolysin are of critical importance to its enzymatic function. The active residue is a glutamate amino acid located at the 145th position of the protein.
Aureolysin