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Gulosibacter molinativorax ON4T Molinate Hydrolase, a Novel Cobalt-Dependent Amidohydrolase ▿ ‡

By Márcia Duarte, Frederico Ferreira-da-Silva, Heinrich Lünsdorf, Howard Junca, Luís Gales, Dietmar H. Pieper and Olga C. Nunes

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 ON4T 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

Topics: Enzymes and Proteins
Publisher: American Society for Microbiology
OAI identifier: oai:pubmedcentral.nih.gov:3187197
Provided by: PubMed Central
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