Isolation of propioxatin A from Actinosynnema sp. SI-23 during a screening for Serratia piscatorum metalloproteinase inhibitors.
An inhibitor of Serratia metalloproteinase was found in the cultured broth of strain SI-23, which was identified to be Actinosynnema sp. The inhibitor had a potent inhibitory effect on Serratia metalloproteinase and a weak effect on thermolysin, but no effect on other groups of proteinases. The structure of the inhibitor was deduced to be propioxatin A, reported as an enkephalinase B inhibitor.
Murao
S
S
Department of Applied Microbial Technology, Kumamoto Institute of Technology, Japan.
Imafuku
S
S
Oyama
H
H
D000192:Actinomycetales / Q000737:chemistry*; D002851:Chromatography, High Pressure Liquid; D002855:Chromatography, Thin Layer; D003470:Culture Media; D004151:Dipeptides / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D006868:Hydrolysis; D009682:Magnetic Resonance Spectroscopy; D008666:Metalloendopeptidases / Q000037:antagonists & inhibitors*; D011480:Protease Inhibitors / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D012705:Serratia / Q000201:enzymology*
D003470:Culture Media; D004151:Dipeptides; D011480:Protease Inhibitors; C050683:propioxatin A; D008666:Metalloendopeptidases