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

• Type: Article in International Scientific Journal
• Date: 2011

Authors

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

Journal

Title: Journal of Bacteriology

Vol. 193 No. 20

Pages: 5810-5816

ISSN: 0021-9193

Publisher: American Society for Microbiology

Indexing

ISI Web of Knowledge - 20 Citations

Scopus - 19 Citations

Scientific classification

FOS: Natural sciences > Biological sciences

CORDIS: Technological sciences > Engineering > Chemical engineering ; Natural sciences > Biological sciences > Biology > Microbiology

Other information

Authenticus ID: 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.

Language: English

Type (Professor's evaluation): Scientific

No. of pages: 7