Novel metal-binding site of Pseudomonas reinekei MT1 trans-dienelactone hydrolase.
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AbstractPseudomonasreinekei MT1 is capable of growing on 4- and 5-chlorosalicylate as the sole carbon source involving a pathway with trans-dienelactone hydrolase as the key enzyme. This enzyme transforms 4-chloromuconolactone to maleylacetate and thereby avoids the spontaneous formation of toxic protoanemonin. trans-Dienelactone hydrolase is a Zn(2+)-dependent hydrolase where activity can be modulated by the exchange of Zn(2+) by Mn(2+) in at least two of the three metal-binding sites. Site directed variants of conserved residues of the Q(101)XXXQ(105)XD(107)XXXH(111) motif and of H281 and E294 exhibit a two order of magnitude decrease in activity and a strong decrease in metal-binding capability. As none of the variants exhibited a change in secondary structure, the analyzed amino acid residues can be assumed to be involved in metal binding, forming a novel trinuclear metal-binding motif.
CitationNovel metal-binding site of Pseudomonas reinekei MT1 trans-dienelactone hydrolase. 2009, 390 (4):1345-8 Biochem. Biophys. Res. Commun.
AffiliationDivision of Microbial Pathogenesis, HZI - Helmholtz Centre for Infection Research, Inhoffenstr. 7, 38124 Braunschweig, Germany.
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- trans-Dienelactone hydrolase from Pseudomonas reinekei MT1, a novel zinc-dependent hydrolase.
- Authors: Cámara B, Marín M, Schlömann M, Hecht HJ, Junca H, Pieper DH
- Issue date: 2008 Nov 14
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