ArticleProteins2021
Catalytic and structural properties of ATP-dependent caprolactamase from Pseudomonas jessenii.
Article in Proteins, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 9 citations in OpenAlex.
- Beyond the β-α-β Fold: Characterization of a SnoaL Domain in the Tautomerase Superfamily.Biochemistry · 2025Article
- Mild hydrolysis of chemically stable valerolactams by a biocatalytic ATP-dependent system fueled by metaphosphate.Green chemistry : an international journal and green chemistry resource : GC · 2024Article
- Interactome Analysis Identifies MSMEI_3879 as a Substrate of Mycolicibacterium smegmatis ClpC1.Microbiology spectrum · 2023Article
- In silico prediction of the enzymes involved in the degradation of the herbicide molinate by Gulosibacter molinativorax ON4Scientific reports · 2022Article
- Transcript profiling of glutathione metabolizing genes reveals abiotic stress and glutathione-specific alteration inPhysiology and molecular biology of plants : an international journal of functional plant biology · 2022Article
- Catalytic and structural properties of ATP-dependent caprolactamase from Pseudomonas jessenii.Proteins · 2021Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Caprolactamase is the first enzyme in the caprolactam degradation pathway of Pseudomonas jessenii. It is composed of two subunits (CapA and CapB) and sequence-related to other ATP-dependent enzymes involved in lactam hydrolysis, like 5-oxoprolinases and hydantoinases. Low sequence similarity also exists with ATP-dependent acetone- and acetophenone carboxylases. The caprolactamase was produced in Escherichia coli, isolated by His-tag affinity chromatography, and subjected to functional and structural studies. Activity toward caprolactam required ATP and was dependent on the presence of bicarbonate in the assay buffer. The hydrolysis product was identified as 6-aminocaproic acid. Quantum mechanical modeling indicated that the hydrolysis of caprolactam was highly disfavored (ΔG
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Registered trials
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