کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
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1934823 | 1050651 | 2008 | 6 صفحه PDF | دانلود رایگان |

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 Zn2+ or Mn2+. Thus, trans-DLH is a Zn2+-dependent hydrolase using halosubstituted muconolactones and trans-dienelactone as substrates, where Mn2+ can substitute for Zn2+. It is the first member of COG1878 and PF04199 for which a direct physiological function has been reported.
Journal: Biochemical and Biophysical Research Communications - Volume 376, Issue 2, 14 November 2008, Pages 423–428