Two aminopeptidases (arylamidases) were isolated and partially purified from Histoplasma capsulatum. The larger molecular weight enzyme was a proline iminopeptidase and hydrolyzed primarily a synthetic substrate, L-prolyl-βnapthylamide. The other aminopeptidase was less substrate specific and hydrolyzed rapidly the following amino acid βnapthylamides (βNA): L-arginyl-βNA > L-lysyl-βNA > L-4-Methoxy-leucyl-βNA > L-leucyl-βNA > L-phenylalanyl-βNA>L-alanyl-βNA. The proline iminopeptidase was purified 1420 fold while the leucine aminopeptidase was purified 650 fold with good recovery.
ASJC Scopus subject areas
- Infectious Diseases