Gulosibacter molinativorax ON4T molinate hydrolase, a novel cobalt-dependent amidohydrolase.
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Authors
Duarte, MárciaFerreira-da-Silva, Frederico
Lünsdorf, Heinrich
Junca, Howard
Gales, Luís
Pieper, Dietmar H
Nunes, Olga C
Issue Date
2011-10
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Show full item recordAbstract
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 bacteriologyPubMed ID
21840982Type
ArticleLanguage
enISSN
1098-5530ae974a485f413a2113503eed53cd6c53
10.1128/JB.05054-11
Scopus Count
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