Biological and Pharmaceutical Bulletin
Online ISSN : 1347-5215
Print ISSN : 0918-6158
ISSN-L : 0918-6158
Involvement of a Novel Mouse Hepatic Microsomal Esterase, ES46.5K, in the Hydrolysis of Phthalate Esters
Yuichiro KAYANOKazuhito WATANABETamihide MATSUNAGAIkuo YAMAMOTOHidetoshi YOSHIMURA
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1997 Volume 20 Issue 7 Pages 749-751

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Abstract

ES46.5K, a novel esterase from mouse hepatic microsomes (Watanabe K., et al., Biochem. Mol. Biol. Int., 31, 25-30 (1993)), catalyzed hydrolysis of phthalate esters. ES46.5K and mouse hepatic microsomes hydrolyzed diethyl-, dibutyl-, diisobutyl-, dioctyl- and diethylhexyl phthalates, whereas dicyclohexyl- and diphenyl phthalates having ring structure were not hydrolyzed by the enzymes. Vmax (μmol/min/mg protein)/Km (μM) ratios of ES46.5K for diethyl-, dibutyl-, diisobutyl-, dioctyl- and diethylhexyl phthalates were 291, 2786, 565, 51 and 57, respectively, while those of microsomes were 0.58, 0.83, 1.71, 0.05 and 1.10, respectively. The hydrolytic activity of ES46.5K was inhibited by diisopropylfluorophosphate and bis-p-nitrophenylphosphate. These results suggest that ES46.5K has high catalytic activity for phthalate esters and some role in the metabolism of phthalate esters in mice.

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