ArticleMolecules (Basel, Switzerland)2017
Structural Basis for the Substrate Inhibition of Proline Utilization A by Proline.
Article in Molecules (Basel, Switzerland), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 15 citations in OpenAlex.
- Plasma lipids, amino acids, and their metabolic pathways as potential biomarkers for differential diagnosis of cold and heat syndrome asthma in children: a preliminary study.Frontiers in pediatrics · 2025Article
- Proline utilization A controls bacterial pathogenicity by sensing its substrate and cofactors.Communications biology · 2022Article
- Photoinduced Covalent Irreversible Inactivation of Proline Dehydrogenase by S-Heterocycles.ACS chemical biology · 2021Article
- Structural basis for the stereospecific inhibition of the dual proline/hydroxyproline catabolic enzyme ALDH4A1 by trans-4-hydroxy-L-proline.Protein science : a publication of the Protein Society · 2021Article
- Structural analysis of prolines and hydroxyprolines binding to the l-glutamate-γ-semialdehyde dehydrogenase active site of bifunctional proline utilization A.Archives of biochemistry and biophysics · 2021Article
- Covalent Modification of the Flavin in Proline Dehydrogenase by Thiazolidine-2-Carboxylate.ACS chemical biology · 2020Article
- Special Issue: Flavoenzymes.Molecules (Basel, Switzerland) · 2018Article
- Redox Modulation of Oligomeric State in Proline Utilization A.Biophysical journal · 2018Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Proline utilization A (PutA) is a bifunctional flavoenzyme that catalyzes the two-step oxidation of l-proline to l-glutamate using spatially separated proline dehydrogenase (PRODH) and l-glutamate-γ-semialdehyde dehydrogenase (GSALDH) active sites. Substrate inhibition of the coupled PRODH-GSALDH reaction by proline is a common kinetic feature of PutAs, yet the structural basis for this phenomenon remains unknown. To understand the mechanism of substrate inhibition, we determined the 2.15 Å resolution crystal structure of
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Registered trials
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