ArticleApplied and environmental microbiology2015
Evolutionary expansion of the amidohydrolase superfamily in bacteria in response to the synthetic compounds molinate and diuron.
Article in Applied and environmental microbiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 38 citations in OpenAlex.
- A previously unappreciated class of metal-dependent bile salt hydrolases from the human gut microbiome.bioRxiv : the preprint server for biology · 2026Article
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- Proteomic characterization ofFrontiers in microbiology · 2026Article
- A new amidohydrolase and β-oxidation-like pathway for piperine catabolism in soil actinomycetes.The Journal of biological chemistry · 2025Article
- Molecular insights into ochratoxin A biodegradation.Biologia futura · 2025Review
- A Thermostable Bacterial Metallohydrolase that Degrades Organophosphate Plasticizers.Chembiochem : a European journal of chemical biology · 2025Article
- Revisiting D-Acylases for D-Amino Acid Production.Microbial biotechnology · 2025Article
- Substrate Specificities of Variants of Barley (1,3)- and (1,3;1,4)-β-d-Glucanases Resulting from Mutagenesis and Segment Hybridization.Biochemistry · 2024Article
- Bioinformatic Analysis of Sulfotransferases from an Unexplored Gut Microbe,International journal of molecular sciences · 2024Article
- Retracing the Rapid Evolution of an Herbicide-Degrading Enzyme by Protein Engineering.ACS catalysis · 2023Article
- In silico prediction of the enzymes involved in the degradation of the herbicide molinate by Gulosibacter molinativorax ON4Scientific reports · 2022Article
- Whole Genome Sequencing and TnInternational journal of molecular sciences · 2020Article
- Delving into the Characteristic Features of "Menace" Mycobacterium tuberculosis Homologs: A Structural Dynamics and Proteomics Perspectives.The protein journal · 2020Article
- Characterization and Crystal Structure of a Nonheme Diiron Monooxygenase Involved in Platensimycin and Platencin Biosynthesis.Journal of the American Chemical Society · 2019Article
- Diuron tolerance and potential degradation by pelagic microbiomes in the Great Barrier Reef lagoon.PeerJ · 2016Article
- Diversity in protein domain superfamilies.Current opinion in genetics & development · 2015Review
- X-Ray Structure and Mutagenesis Studies of the N-Isopropylammelide Isopropylaminohydrolase, AtzC.PloS one · 2015Article
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Authors and funding
8 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The amidohydrolase superfamily has remarkable functional diversity, with considerable structural and functional annotation of known sequences. In microbes, the recent evolution of several members of this family to catalyze the breakdown of environmental xenobiotics is not well understood. An evolutionary transition from binuclear to mononuclear metal ion coordination at the active sites of these enzymes could produce large functional changes such as those observed in nature, but there are few clear examples available to support this hypothesis. To investigate the role of binuclear-mononuclear active-site transitions in the evolution of new function in this superfamily, we have characterized two recently evolved enzymes that catalyze the hydrolysis of the synthetic herbicides molinate (MolA) and phenylurea (PuhB). In this work, the crystal structures, mutagenesis, metal ion analysis, and enzyme kinetics of both MolA and PuhB establish that these enzymes utilize a mononuclear active site. However, bioinformatics and structural comparisons reveal that the closest putative ancestor of these enzymes had a binuclear active site, indicating that a binuclear-mononuclear transition has occurred. These proteins may represent examples of evolution modifying the characteristics of existing catalysts to satisfy new requirements, specifically, metal ion rearrangement leading to large leaps in activity that would not otherwise be possible.
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