ArticleBiochemistry and biophysics reports2016
Isothermal titration calorimetry uncovers substrate promiscuity of bicupin oxalate oxidase from
Article in Biochemistry and biophysics reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
3 citing papers in PubMed, 13 citations in OpenAlex.
- Carbon Nanotube PtSn Nanoparticles for Enhanced Complete Biocatalytic Oxidation of Ethylene Glycol in Biofuel Cells.ACS materials Au · 2022Article
- Quantifying the flux as the driving force for nonequilibrium dynamics and thermodynamics in non-Michaelis-Menten enzyme kinetics.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Hydrogen peroxide inhibition of bicupin oxalate oxidase.PloS one · 2017Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Isothermal titration calorimetry (ITC) may be used to determine the kinetic parameters of enzyme-catalyzed reactions when neither products nor reactants are spectrophotometrically visible and when the reaction products are unknown. We report here the use of the multiple injection method of ITC to characterize the catalytic properties of oxalate oxidase (OxOx) from
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Registered trials
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