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Biochem Biophys Res Commun. 2008 Nov 14;376(2):423-8. doi: 10.1016/j.bbrc.2008.09.006. Epub 2008 Sep 17.

trans-Dienelactone hydrolase from Pseudomonas reinekei MT1, a novel zinc-dependent hydrolase.

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  • 1Department of Microbial Pathogenesis, HZI-Helmholtz Centre for Infection Research, Inhoffenstr. 7, 38124 Braunschweig, Germany.


Pseudomonas reinekei MT1 is capable of growing on 4- and 5-chlorosalicylate, involving a pathway with trans-dienelactone hydrolase (trans-DLH) as a key enzyme. It acts on 4-chloromuconolactone formed during cycloisomerization of 3-chloromuconate by hydrolyzing it to maleylacetate. The gene encoding this activity was localized, sequenced and expressed in Escherichia coli. Inductively coupled plasma mass spectrometry showed that both the wild-type as well as recombinant enzymes contained 2 moles of zinc but variable amounts of manganese/mol of protein subunit. The inactive metal-free apoenzyme could be reactivated by Zn(2+) or Mn(2+). Thus, trans-DLH is a Zn(2+)-dependent hydrolase using halosubstituted muconolactones and trans-dienelactone as substrates, where Mn(2+) can substitute for Zn(2+). It is the first member of COG1878 and PF04199 for which a direct physiological function has been reported.

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