Structural basis for the inactivation of Thermus thermophilus proline dehydrogenase by N-propargylglycine.
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Summary
The first crystal structure of an irreversibly inactivated proline dehydrogenase is reported, showing that N5 of the flavin cofactor is covalently connected to the -amino group of Lys99 via a three-carbon linkage, consistent with the mass spectral analysis of the inactivated enzyme.
- Type
- article
- Published
- 2008-04-22
- Cited by
- 31
- References
- 48
- Access
- Open access
- OpenAlex
- https://openalex.org/W2012655528
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:295521
Keywords
Thermus thermophilus, Flavin group, Chemistry, Stereochemistry, Cofactor
References
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- Biochemical adaptations for flight in the insect.
- Flavin suicide inhibitor adducts.
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- Macromolecular TLS refinement in REFMAC at moderate resolutions.
- Esters of methanesulfonic acid as irreversible inhibitors of acetylcholinesterase.
- Redesigned purification yields a fully functional PutA protein dimer from Escherichia coli.
- A model for p53-induced apoptosis
- Mechanism-based enzyme inactivators.
- Stoichiometric estimates of the biochemical conversion efficiencies in tsetse metabolism
- Proline dehydrogenase from Escherichia coli K12. Properties of the membrane-associated enzyme.
- Proline Oxidase, a Proapoptotic Gene, Is Induced by Troglitazone
- The p53-induced Gene-6 (Proline Oxidase) Mediates Apoptosis through a Calcineurin-dependent Pathway*
- Effects of proline analog binding on the spectroscopic and redox properties of PutA.
- Regulation of proline oxidase activity by lactate.
- PROCHECK: a program to check the stereochemical quality of protein structures
- Binding of rasagiline-related inhibitors to human monoamine oxidases: a kinetic and crystallographic analysis.
- Proline Oxidase Induces Apoptosis in Tumor Cells, and Its Expression Is Frequently Absent or Reduced in Renal Carcinomas*
- Structure and Kinetics of Monofunctional Proline Dehydrogenase from Thermus thermophilus*
- Structural biology of proline catabolism
Cited by
- Substrate channeling in proline metabolism
- Investigations of substrate channeling in the proline oxidative pathway
- Unique Structural Features and Sequence Motifs of Proline Utilization A (PutA)
- Diethylaminobenzaldehyde is a covalent, irreversible inactivator of ALDH7A1.
- Structures of the PutA peripheral membrane flavoenzyme reveal a dynamic substrate-channeling tunnel and the quinone-binding site
- Structural biology of proline catabolism
- Crystal Structures and Kinetics of Monofunctional Proline Dehydrogenase Provide Insight into Substrate Recognition and Conformational Changes Associated With Flavin Reduction and Product Release
- A Conserved Active Site Tyrosine Residue of Proline Dehydrogenase Helps Enforce the Preference for Proline over Hydroxyproline as the Substrate,
- 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,
- Three crystal forms of the bifunctional enzyme proline utilization A (PutA) from Bradyrhizobium japonicum.
- Trimming proline dehydrogenase : protein and cofactor minimization
- Biophysical investigation of type A PutAs reveals a conserved core oligomeric structure
- Structural Biology of Proline Catabolic Enzymes
- Structural Basis for the Substrate Inhibition of Proline Utilization A by Proline
- Functional Impact of the N-terminal Arm of Proline Dehydrogenase from Thermus thermophilus
- The Proline Cycle As a Potential Cancer Therapy Target
- Redox Modulation of Oligomeric State in Proline Utilization A.
- Targeting mitochondrial proline dehydrogenase with a suicide inhibitor to exploit synthetic lethal interactions with p53 upregulation and glutaminase inhibition
- Covalent Modification of the Flavin in Proline Dehydrogenase by Thiazolidine-2-Carboxylate
- N-Propargylglycine: a unique suicide inhibitor of proline dehydrogenase with anticancer activity and brain-enhancing mitohormesis properties
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