Structural Basis for the Substrate Inhibition of Proline Utilization A by Proline
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Summary
Structural and kinetic data show that substrate inhibition of the PutA coupled reaction is due to proline binding in the GSAL site, implying that proline inhibits theGSALDH reaction of PutA.
- Type
- article
- Published
- 2017-12-23
- Cited by
- 13
- References
- 32
- Access
- Open access
- OpenAlex
- https://openalex.org/W2779352078
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:5234577
Keywords
Proline dehydrogenase, Proline, Active site, Chemistry, Substrate (aquarium)
References
- Structural Basis of Substrate Recognition by Aldehyde Dehydrogenase 7A1
- Human glutamic-gamma-semialdehyde dehydrogenase. Kinetic mechanism.
- Evidence for Hysteretic Substrate Channeling in the Proline Dehydrogenase and Δ1-Pyrroline-5-carboxylate Dehydrogenase Coupled Reaction of Proline Utilization A (PutA)*
- Structures of the PutA peripheral membrane flavoenzyme reveal a dynamic substrate-channeling tunnel and the quinone-binding site
- Structure and Kinetics of Monofunctional Proline Dehydrogenase from Thermus thermophilus*
- Structural determinants of substrate specificity in aldehyde dehydrogenases.
- Structural basis for the inactivation of Thermus thermophilus proline dehydrogenase by N-propargylglycine.
- Solvent content of protein crystals.
- Structures of the Escherichia coli PutA proline dehydrogenase domain in complex with competitive inhibitors.
- Crystal Structures and Kinetics of Monofunctional Proline Dehydrogenase Provide Insight into Substrate Recognition and Conformational Changes Associated With Flavin Reduction and Product Release
- Improved chemical synthesis and enzymatic assay of delta-1-pyrroline-5-carboxylic acid.
- Steady-State Kinetic Mechanism of the Proline:Ubiquinone Oxidoreductase Activity of Proline Utilization A (PutA) from Escherichia coli
- The Three-Dimensional Structural Basis of Type II Hyperprolinemia
- A Conserved Active Site Tyrosine Residue of Proline Dehydrogenase Helps Enforce the Preference for Proline over Hydroxyproline as the Substrate,
- Crystal structure of Thermus thermophilus Delta1-pyrroline-5-carboxylate dehydrogenase.
- Structure of the Proline Utilization A Proline Dehydrogenase Domain Inactivated by N-propargylglycine Provides Insight into Conformational Changes Induced by Substrate Binding and Flavin Reduction,
- Crystal structure of the bifunctional proline utilization A flavoenzyme from Bradyrhizobium japonicum
- Three crystal forms of the bifunctional enzyme proline utilization A (PutA) from Bradyrhizobium japonicum.
- Structure of the proline dehydrogenase domain of the multifunctional PutA flavoprotein
- Proline: Mother Nature's cryoprotectant applied to protein crystallography.
Cited by
- Redox Modulation of Oligomeric State in Proline Utilization A.
- Structure–function relationships of the 5‐oxoprolinase subunit A: Guiding biological sciences students down the path less traveled
- Determining a suitable carbon source for the production of intracellular pigments from Monascus purpureus HBSD 08
- Effects of hypertension and FAAH inhibitor treatment of rats with primary and secondary hypertension considering the physicochemical properties of erythrocytes
- Covalent Modification of the Flavin in Proline Dehydrogenase by Thiazolidine-2-Carboxylate
- Structural Analysis of Prolines and Hydroxyprolines Binding to the L-glutamate-γ-semialdehyde Dehydrogenase Active Site of Bifunctional Proline Utilization A
- Structural basis for the stereospecific inhibition of the dual proline/hydroxyproline catabolic enzyme ALDH4A1 by trans‐4‐hydroxy‐L‐proline
- A catalogue of signal molecules that interact with sensor kinases, chemoreceptors and transcriptional regulators.
- Photoinduced Covalent Irreversible Inactivation of Proline Dehydrogenase by S-Heterocycles
- Proline utilization A controls bacterial pathogenicity by sensing its substrate and cofactors
- 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
- Special Issue: Flavoenzymes
- Special Issue: Flavoenzymes.
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