ArticleThe Journal of biological chemistry2014
A proton wire and water channel revealed in the crystal structure of isatin hydrolase.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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12 citing papers in PubMed, 23 citations in OpenAlex.
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- Marine-derived fungi as biocatalysts.Frontiers in microbiology · 2023Review
- Utilization of diverse organophosphorus pollutants by marine bacteria.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- True-atomic-resolution insights into the structure and functional role of linear chains and low-barrier hydrogen bonds in proteins.Nature structural & molecular biology · 2022Article
- Discovery and Optimization of Inhibitors of the Parkinson's Disease Associated Protein DJ-1.ACS chemical biology · 2018Article
- A fundamental catalytic difference between zinc and manganese dependent enzymes revealed in a bacterial isatin hydrolase.Scientific reports · 2018Article
- Biodegradation and Biotransformation of Indole: Advances and Perspectives.Frontiers in microbiology · 2018Review
- Activity screening of environmental metagenomic libraries reveals novel carboxylesterase families.Scientific reports · 2017Article
- Metabolic Pathway Involved in 6-Chloro-2-Benzoxazolinone Degradation by Pigmentiphaga sp. Strain DL-8 and Identification of the Novel Metal-Dependent Hydrolase CbaA.Applied and environmental microbiology · 2016Article
- A 2-Hydroxypyridine Catabolism Pathway in Rhodococcus rhodochrous Strain PY11.Applied and environmental microbiology · 2016Article
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Authors and funding
6 authors at 2 institutions in 2 countries.
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No grant is acknowledged in the PubMed record.
Abstract
The high resolution crystal structures of isatin hydrolase from Labrenzia aggregata in the apo and the product state are described. These are the first structures of a functionally characterized metal-dependent hydrolase of this fold. Isatin hydrolase converts isatin to isatinate and belongs to a novel family of metalloenzymes that include the bacterial kynurenine formamidase. The product state, mimicked by bound thioisatinate, reveals a water molecule that bridges the thioisatinate to a proton wire in an adjacent water channel and thus allows the proton released by the reaction to escape only when the product is formed. The functional proton wire present in isatin hydrolase isoform b represents a unique catalytic feature common to all hydrolases is here trapped and visualized for the first time. The local molecular environment required to coordinate thioisatinate allows stronger and more confident identification of orthologous genes encoding isatin hydrolases within the prokaryotic kingdom. The isatin hydrolase orthologues found in human gut bacteria raise the question as to whether the indole-3-acetic acid degradation pathway is present in human gut flora.
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