ArticleProtein science : a publication of the Protein Society2019
A cryptic activity in the Nudix hydrolase superfamily.
Article in Protein science : a publication of the Protein Society, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 24 citations in OpenAlex.
- Clinical correlations and prognostic value of Nudix hydroxylase 10 in patients with gastric cancer.Bioengineered · 2021Trial
- Article
- Metabolic Origin, Role and Fate of the Denaturant Guanidine.Microbial biotechnology · 2025Article
- Antimutator and Mutational Spectrum Effects Can Combine to Reduce Evolutionary Potential in Escherichia coli ΔnudJ.Molecular biology and evolution · 2025Article
- Optimization of a high throughput screening platform to identify inhibitors of asymmetric diadenosine polyphosphatases.Analytical biochemistry · 2025Article
- Investigation of the Structure and Functional Activity of the YqeK Protein inMicroorganisms · 2025Article
- The F plasmid conjutome: the repertoire ofmSphere · 2024Article
- The Lreu_1276 protein fromApplied and environmental microbiology · 2024Article
- Phosphorus Acquisition Efficiency and Transcriptomic Changes in Maize Plants Treated with Two Lignohumates.Plants (Basel, Switzerland) · 2023Article
- Transcriptome profiling of Nudix hydrolase gene deletions in the thermoacidophilic archaeonFrontiers in microbiology · 2023Article
- NADAnimal nutrition (Zhongguo xu mu shou yi xue hui) · 2022Review
- Structural Insight into Molecular Inhibitory Mechanism of InsPJournal of virology · 2022Article
- Construction of m7G subtype classification on heterogeneity of sepsis.Frontiers in genetics · 2022Article
- Fluorescent probe displacement assays reveal unique nucleic acid binding properties of human nudix enzymes.Analytical biochemistry · 2020Article
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Authors and funding
1 author at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Nudix hydrolase superfamily is identified by a conserved cassette of 23 amino acids, and it is characterized by its pyrophosphorylytic activity on a wide variety of nucleoside diphosphate derivatives. Of the 13 members of the family in Escherichia coli, only one, Orf180, has not been identified with a substrate, although a host of nucleoside diphosphate compounds has been tested. Several reports have noted a strong similarity in the three-dimensional structure of the unrelated enzyme, isopentenyl diphosphate isomerase (IDI) to the Nudix structure, and the report that a Nudix enzyme was involved in the synthesis of geraniol, a product of the two substrates of IDI, prompted an investigation of whether the IDI substrates, isopentenyl diphosphate (IPP), and dimethylallyl diphosphate (DAPP) could be substrates of Orf180. This article demonstrates that Orf180 does have a very low activity on IPP, DAPP, and geranyl pyrophosphate (GPP). However, several of the other Nudix enzymes with established nucleoside diphosphate substrates hydrolyze these compounds at substantial rates. In fact, some Nudix hydrolases have higher activities on IPP, DAPP, and GPP than on their signature nucleoside diphosphate derivatives.
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