Actinomycin D inactivating enzymes fromActinoplanes missouriensis and several other members of theActinoplanaceae family

Summary The enzymes for inactivating actinomycin D appear to be widely distributed amongst species belonging to the familyActinoplanaceae. Actinomycin D was completely or partially inactivated by cell-free extracts fromActinoplanes missouriensis, Streptosporangium viridogriseum, S. violaceocbromogenes, S. roseum, S. brasiliense, S. albidum, Spirillospora sp.,Sp. albida, Kitasatoa kauaiensis, Planobispora longispora, P. rosea, Dactylosporangium aurantiacum, andD. thailandense. No inactivation was obtained with extracts fromAmorphosphorangium auranticolor, Ampullariella lobata, Planomonospora parontospora, andP. venezuelensis. Actinomycin lactonase was partially purified by ultracentrifugation, ultrafiltration, and isoelectric focusing from noninduced cells ofActinoplanes missouriensis. The enzyme has a molecular weight of greater than 200,000 daltons and an isoelectric point of 4.3 to 4.4.