ArticleJournal of bacteriology2011
Gulosibacter molinativorax ON4T molinate hydrolase, a novel cobalt-dependent amidohydrolase.
Article in Journal of bacteriology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 22 citations in OpenAlex.
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- Vitamin BACS central science · 2025Article
- A new amidohydrolase and β-oxidation-like pathway for piperine catabolism in soil actinomycetes.The Journal of biological chemistry · 2025Article
- In silico prediction of the enzymes involved in the degradation of the herbicide molinate by Gulosibacter molinativorax ON4Scientific reports · 2022Article
- Exploring the substrate scope of ferulic acid decarboxylase (FDC1) from Saccharomyces cerevisiae.Scientific reports · 2019Article
- QM Cluster or QM/MM in Computational Enzymology: The Test Case of LigW-Decarboxylase.Frontiers in chemistry · 2018Article
- Evolutionary expansion of the amidohydrolase superfamily in bacteria in response to the synthetic compounds molinate and diuron.Applied and environmental microbiology · 2015Article
- Structure-guided engineering of molinate hydrolase for the degradation of thiocarbamate pesticides.PloS one · 2015Article
- HylA, an alternative hydrolase for initiation of catabolism of the phenylurea herbicide linuron in Variovorax sp. strains.Applied and environmental microbiology · 2013Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
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.
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