2.50
Hdl Handle:
http://hdl.handle.net/10033/88753
Title:
Novel metal-binding site of Pseudomonas reinekei MT1 trans-dienelactone hydrolase.
Authors:
Marín, Macarena; Pieper, Dietmar H
Abstract:
Pseudomonasreinekei 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.
Affiliation:
Division of Microbial Pathogenesis, HZI - Helmholtz Centre for Infection Research, Inhoffenstr. 7, 38124 Braunschweig, Germany.
Citation:
Novel metal-binding site of Pseudomonas reinekei MT1 trans-dienelactone hydrolase. 2009, 390 (4):1345-8 Biochem. Biophys. Res. Commun.
Journal:
Biochemical and biophysical research communications
Issue Date:
25-Dec-2009
URI:
http://hdl.handle.net/10033/88753
DOI:
10.1016/j.bbrc.2009.10.151
PubMed ID:
19895788
Type:
Article
Language:
en
ISSN:
1090-2104
Appears in Collections:
Publications of RG Mikrobielle Interaktionen und Prozesse (MINP)

Full metadata record

DC FieldValue Language
dc.contributor.authorMarín, Macarenaen
dc.contributor.authorPieper, Dietmar Hen
dc.date.accessioned2010-01-05T13:12:47Z-
dc.date.available2010-01-05T13:12:47Z-
dc.date.issued2009-12-25-
dc.identifier.citationNovel metal-binding site of Pseudomonas reinekei MT1 trans-dienelactone hydrolase. 2009, 390 (4):1345-8 Biochem. Biophys. Res. Commun.en
dc.identifier.issn1090-2104-
dc.identifier.pmid19895788-
dc.identifier.doi10.1016/j.bbrc.2009.10.151-
dc.identifier.urihttp://hdl.handle.net/10033/88753-
dc.description.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.en
dc.language.isoenen
dc.titleNovel metal-binding site of Pseudomonas reinekei MT1 trans-dienelactone hydrolase.en
dc.typeArticleen
dc.contributor.departmentDivision of Microbial Pathogenesis, HZI - Helmholtz Centre for Infection Research, Inhoffenstr. 7, 38124 Braunschweig, Germany.en
dc.identifier.journalBiochemical and biophysical research communicationsen

Related articles on PubMed

This item is licensed under a Creative Commons License
Creative Commons
All Items in HZI are protected by copyright, with all rights reserved, unless otherwise indicated.