2.50
Hdl Handle:
http://hdl.handle.net/10033/344586
Title:
Gulosibacter molinativorax ON4T molinate hydrolase, a novel cobalt-dependent amidohydrolase.
Authors:
Duarte, Márcia; Ferreira-da-Silva, Frederico; Lünsdorf, Heinrich; Junca, Howard ( 0000-0003-4546-6229 ) ; Gales, Luís; Pieper, Dietmar H; Nunes, Olga C
Abstract:
A new pathway of molinate mineralization has recently been described. Among the five members of the mixed culture able to promote such a process, Gulosibacter molinativorax ON4(T) has been observed to promote the initial breakdown of the herbicide into ethanethiol and azepane-1-carboxylate. In the current study, the gene encoding the enzyme responsible for molinate hydrolysis was identified and heterologously expressed, and the resultant active protein was purified and characterized. Nucleotide sequence analysis revealed that the gene encodes a 465-amino-acid protein of the metal-dependent hydrolase A subfamily of the amidohydrolase superfamily with a predicted molecular mass of 50.9 kDa. Molinate hydrolase shares the highest amino acid sequence identity (48 to 50%) with phenylurea hydrolases of Arthrobacter globiformis and Mycobacterium brisbanense. However, in contrast to previously described members of the metal-dependent hydrolase A subfamily, molinate hydrolase contains cobalt as the only active-site metal.
Citation:
Gulosibacter molinativorax ON4T molinate hydrolase, a novel cobalt-dependent amidohydrolase. 2011, 193 (20):5810-6 J. Bacteriol.
Journal:
Journal of bacteriology
Issue Date:
Oct-2011
URI:
http://hdl.handle.net/10033/344586
DOI:
10.1128/JB.05054-11
PubMed ID:
21840982
Type:
Article
Language:
en
ISSN:
1098-5530
Appears in Collections:
publications of the research group microbial interactions and processes (MINP)

Full metadata record

DC FieldValue Language
dc.contributor.authorDuarte, Márciaen
dc.contributor.authorFerreira-da-Silva, Fredericoen
dc.contributor.authorLünsdorf, Heinrichen
dc.contributor.authorJunca, Howarden
dc.contributor.authorGales, Luísen
dc.contributor.authorPieper, Dietmar Hen
dc.contributor.authorNunes, Olga Cen
dc.date.accessioned2015-02-19T12:16:43Zen
dc.date.available2015-02-19T12:16:43Zen
dc.date.issued2011-10en
dc.identifier.citationGulosibacter molinativorax ON4T molinate hydrolase, a novel cobalt-dependent amidohydrolase. 2011, 193 (20):5810-6 J. Bacteriol.en
dc.identifier.issn1098-5530en
dc.identifier.pmid21840982en
dc.identifier.doi10.1128/JB.05054-11en
dc.identifier.urihttp://hdl.handle.net/10033/344586en
dc.description.abstractA new pathway of molinate mineralization has recently been described. Among the five members of the mixed culture able to promote such a process, Gulosibacter molinativorax ON4(T) has been observed to promote the initial breakdown of the herbicide into ethanethiol and azepane-1-carboxylate. In the current study, the gene encoding the enzyme responsible for molinate hydrolysis was identified and heterologously expressed, and the resultant active protein was purified and characterized. Nucleotide sequence analysis revealed that the gene encodes a 465-amino-acid protein of the metal-dependent hydrolase A subfamily of the amidohydrolase superfamily with a predicted molecular mass of 50.9 kDa. Molinate hydrolase shares the highest amino acid sequence identity (48 to 50%) with phenylurea hydrolases of Arthrobacter globiformis and Mycobacterium brisbanense. However, in contrast to previously described members of the metal-dependent hydrolase A subfamily, molinate hydrolase contains cobalt as the only active-site metal.en
dc.language.isoenen
dc.subject.meshActinomycetalesen
dc.subject.meshAmidohydrolasesen
dc.subject.meshAmino Acid Sequenceen
dc.subject.meshAzepinesen
dc.subject.meshBacterial Proteinsen
dc.subject.meshCatalytic Domainen
dc.subject.meshCobalten
dc.subject.meshHerbicidesen
dc.subject.meshMolecular Sequence Dataen
dc.subject.meshPhylogenyen
dc.subject.meshSequence Alignmenten
dc.subject.meshThiocarbamatesen
dc.titleGulosibacter molinativorax ON4T molinate hydrolase, a novel cobalt-dependent amidohydrolase.en
dc.typeArticleen
dc.identifier.journalJournal of bacteriologyen

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.