Author： Pinot F. Caldas E.D. Schmidt C. Gilchrist D.G. Jones A.D. Hammock B.D. Winter C.K.
Publisher： Springer Publishing Company
ISSN： 0301-486X
Source： Mycopathologia, Vol.140, Iss.1, 1997-01, pp. : 51-58
Disclaimer: Any content in publications that violate the sovereignty, the constitution or regulations of the PRC is not accepted or approved by CNPIEC.
Abstract
Using trans-diphenylpropane oxide (tDPPO) as a substrate, we measured epoxide hydrolase (EH) activity in subcellular fractions of Alternaria alternata f. sp. lycopersici (Aal), a fungus that produces host-specific toxins. The activity was mainly (>99.5%) located in the soluble fraction (100,000 × g supernatant) with the optimum pH at 7.4. An increase of toxin production between days 3 and 9 found in a Aal liquid culture over a 15 days period was concomitant with a period of high EH activity. EH activity remained constant during the same period in an Alternaria alternata culture, a fungus which does not produce toxin. In vivo treatment of Aal culture with the peroxisome proliferator clofibrate stimulated EH activity by 83% and enhanced toxin production 6.3 fold. Both 4-fluorochalcone oxide (4-FCO) and (2S,3S)-(-)-3-(4-nitrophenyl)-glycidol (SS-NPG) inhibited EH activity in vitro with a IM_50f 23 ± 1 μM and 72 ± 19 μM, respectively. The possible physiological substrate 9,10-epoxystearic acid was hydrolyzed more efficiently by Aal sEH than the model substrates trans- and cis-stilbene oxide (TSO and CSO) and trans- and cis-diphenylpropane oxide (tDPPO and cDPPO).
Related content
By Xu Jianhong Deng Peng Showmaker Kurt C. Wang Hui Baird Sonya M. Lu Shi-En
FEMS Microbiology Letters, Vol. 353, Iss. 2, 2014-04 ,pp. :
Access to resources
Recommend
By Morita Koji Kimura Soichiro Saito Masanori Shinoyama Hirofumi Usami Toshiyuki Amemiya Yoshimiki Shishido Masahiro
Mycopathologia, Vol. 160, Iss. 1, 2005-08 ,pp. :
By Macías-Sánchez Karla García-Soto Jesús López-Ramírez Adriana Martínez-Cadena Guadalupe
Antonie van Leeuwenhoek, Vol. 99, Iss. 3, 2011-03 ,pp. :