Streptomyces griseus Aminopeptidase (SGAP)

From Proteopedia

Streptomyces griseus Aminopeptidase (SGAP)

Biological function

S. griseus Aminopeptidase (SGAP; E.C. 3.4.11.-) cleaves the N-terminal amino acid from a peptide or protein, and is specific for larger hydrophobic acids, especially leucine. No cleavage occurs if the next residue is proline.

Reaction catalyzed by SGAP; scissile bond is shown in red.

Biological Context

SGAP is one of the many proteinases present in the extracellular fluid of cultures of Streptomyces griseus, and can be isolated from Pronase, the commercial preparation of the extracellular fluid from this organism. SGAP is a monomeric, 30KDa, heat stable enzyme requiring two Zn²⁺ ions for activity, and is activated by Ca²⁺.