2.50
HDL Handle:
http://hdl.handle.net/10033/252493
Title:
Degradation of 2,3-dihydroxybenzoate by a novel meta-cleavage pathway.
Authors:
Marín, Macarena; Plumeier, Iris; Pieper, Dietmar H
Abstract:
2,3-Dihydroxybenzoate is the precursor in the biosynthesis of several siderophores and an important plant secondary metabolite that, in bacteria, can be degraded via meta-cleavage of the aromatic ring. The dhb cluster of Pseudomonas reinekei MT1 encodes a chimeric meta-cleavage pathway involved in the catabolism of 2,3-dihydroxybenzoate. While the first two enzymes, DhbA and DhbB, are phylogenetically related to those involved in 2,3-dihydroxy-p-cumate degradation, the subsequent steps are catalyzed by enzymes related to those involved in catechol degradation (DhbCDEFGH). Characterization of kinetic properties of DhbA extradiol dioxygenase identified 2,3-dihydroxybenzoate as the preferred substrate. Deletion of the encoding gene impedes growth of P. reinekei MT1 on 2,3-dihydroxybenzoate. DhbA catalyzes 3,4-dioxygenation with 2-hydroxy-3-carboxymuconate as the product, which is then decarboxylated by DhbB to 2-hydroxymuconic semialdehyde. This compound is then subject to dehydrogenation and further degraded to citrate cycle intermediates. Transcriptional analysis revealed genes of the dhB gene cluster to be highly expressed during growth with 2,3-dihydroxybenzoate, whereas a downstream-localized gene encoding 2-hydroxymuconic semialdehyde hydrolase, dispensable for 2,3-dihydroxybenzoate metabolism but crucial for 2,3-dihydroxy-p-cumate degradation, was only marginally expressed. This is the first report describing a gene cluster encoding enzymes for the degradation of 2,3-dihydroxybenzoate.
Affiliation:
Microbial Interactions and Processes Research Group, HZI-Helmholtz Centre for Infection Research, Braunschweig, Germany.
Citation:
Degradation of 2,3-dihydroxybenzoate by a novel meta-cleavage pathway. 2012, 194 (15):3851-60 J. Bacteriol.
Journal:
Journal of bacteriology
Issue Date:
Aug-2012
URI:
http://hdl.handle.net/10033/252493
DOI:
10.1128/JB.00430-12
PubMed ID:
22609919
Type:
Article
Language:
en
ISSN:
1098-5530
Appears in Collections:
Publications of RG Mikrobielle Interaktionen und Prozesse (MINP)

Full metadata record

DC FieldValueLanguage
dc.contributor.authorMarín, Macarenaen_GB
dc.contributor.authorPlumeier, Irisen_GB
dc.contributor.authorPieper, Dietmar Hen_GB
dc.date.accessioned2012-11-16T14:58:01Z-
dc.date.available2012-11-16T14:58:01Z-
dc.date.issued2012-08-
dc.identifier.citationDegradation of 2,3-dihydroxybenzoate by a novel meta-cleavage pathway. 2012, 194 (15):3851-60 J. Bacteriol.en_GB
dc.identifier.issn1098-5530-
dc.identifier.pmid22609919-
dc.identifier.doi10.1128/JB.00430-12-
dc.identifier.urihttp://hdl.handle.net/10033/252493-
dc.description.abstract2,3-Dihydroxybenzoate is the precursor in the biosynthesis of several siderophores and an important plant secondary metabolite that, in bacteria, can be degraded via meta-cleavage of the aromatic ring. The dhb cluster of Pseudomonas reinekei MT1 encodes a chimeric meta-cleavage pathway involved in the catabolism of 2,3-dihydroxybenzoate. While the first two enzymes, DhbA and DhbB, are phylogenetically related to those involved in 2,3-dihydroxy-p-cumate degradation, the subsequent steps are catalyzed by enzymes related to those involved in catechol degradation (DhbCDEFGH). Characterization of kinetic properties of DhbA extradiol dioxygenase identified 2,3-dihydroxybenzoate as the preferred substrate. Deletion of the encoding gene impedes growth of P. reinekei MT1 on 2,3-dihydroxybenzoate. DhbA catalyzes 3,4-dioxygenation with 2-hydroxy-3-carboxymuconate as the product, which is then decarboxylated by DhbB to 2-hydroxymuconic semialdehyde. This compound is then subject to dehydrogenation and further degraded to citrate cycle intermediates. Transcriptional analysis revealed genes of the dhB gene cluster to be highly expressed during growth with 2,3-dihydroxybenzoate, whereas a downstream-localized gene encoding 2-hydroxymuconic semialdehyde hydrolase, dispensable for 2,3-dihydroxybenzoate metabolism but crucial for 2,3-dihydroxy-p-cumate degradation, was only marginally expressed. This is the first report describing a gene cluster encoding enzymes for the degradation of 2,3-dihydroxybenzoate.en_GB
dc.language.isoenen
dc.rightsArchived with thanks to Journal of bacteriologyen_GB
dc.subject.meshBacterial Proteinsen_GB
dc.subject.meshBiotransformationen_GB
dc.subject.meshDNA, Bacterialen_GB
dc.subject.meshGene Deletionen_GB
dc.subject.meshGene Expression Profilingen_GB
dc.subject.meshGene Orderen_GB
dc.subject.meshHydroxybenzoic Acidsen_GB
dc.subject.meshKineticsen_GB
dc.subject.meshMetabolic Networks and Pathwaysen_GB
dc.subject.meshMolecular Sequence Dataen_GB
dc.subject.meshMultigene Familyen_GB
dc.subject.meshPhylogenyen_GB
dc.subject.meshPseudomonasen_GB
dc.subject.meshSequence Analysis, DNAen_GB
dc.subject.meshSequence Homology, Amino Aciden_GB
dc.subject.meshSubstrate Specificityen_GB
dc.titleDegradation of 2,3-dihydroxybenzoate by a novel meta-cleavage pathway.en
dc.typeArticleen
dc.contributor.departmentMicrobial Interactions and Processes Research Group, HZI-Helmholtz Centre for Infection Research, Braunschweig, Germany.en_GB
dc.identifier.journalJournal of bacteriologyen_GB
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