Gulosibacter molinativorax ON4(T) Molinate Hydrolase, a Novel Cobalt-Dependent Amidohydrolase

• Tipo: Artigo em Revista Científica Internacional
• Data: 2011

Autores

Marcia Duarte (Autor) Outra; Frederico Ferreira da Silva (Autor) Outra; Heinrich Luensdorf (Autor) Outra; Howard Junca (Autor) Outra; Luis Gales (Autor) ICBAS; Dietmar H Pieper (Autor) Outra; Olga C Nunes (Autor) FEUP

Revista

Título: Journal of Bacteriology

Vol. 193 Nº 20

Páginas: 5810-5816

ISSN: 0021-9193

Editora: American Society for Microbiology

Indexação

ISI Web of Knowledge - 20 Citações

Scopus - 19 Citações

Classificação Científica

FOS: Ciências exactas e naturais > Ciências biológicas

CORDIS: Ciências Tecnológicas > Engenharia > Engenharia química ; Ciências Naturais > Ciências biológicas > Biologia > Microbiologia

Outras Informações

ID Authenticus: P-002-M6H

DOI: 10.1128/jb.05054-11

Abstract (EN): 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.

Idioma: Inglês

Tipo (Avaliação Docente): Científica

Nº de páginas: 7