| Primary Identifier | IPR041756 | Type | Family |
| Short Name | M28_SGAP-like |
| description | This entry represents the Streptomyces griseus Aminopeptidase (SGAP, Leucine aminopeptidase (LAP), aminopeptidase S, Mername-AA022 peptidase) subfamily of the peptidase family M28. SGAP is a di-zinc exopeptidase with high preference towards large hydrophobic amino-terminal residues, with Leu being the most efficiently cleaved []. It can accommodate all except Pro and Glu residues in the P1' position. It is a monomeric (30kDa), calcium-activated and calcium-stabilized enzyme; its activation by calcium correlates with substrate specificity and it has thermal stability only in the presence of calcium. Although SGAP contains a calcium binding site, it is not conserved in many members of this subfamily. SGAP is present in the extracellular fluid of S. griseus cultures [, ]. |
