ArticleBiochemistry2014
Kinetic and structural characterization of tunnel-perturbing mutants in Bradyrhizobium japonicum proline utilization A.
Article in Biochemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 20 citations in OpenAlex.
- Noncovalent Inhibition and Covalent Inactivation of Proline Dehydrogenase by Analogs ofBiochemistry · 2024Article
- Proline Dehydrogenase and Pyrroline 5 Carboxylate Dehydrogenase fromPathogens (Basel, Switzerland) · 2023Article
- Evidence for Proline Catabolic Enzymes in the Metabolism of Thiazolidine Carboxylates.Biochemistry · 2021Article
- Probing the function of a ligand-modulated dynamic tunnel in bifunctional proline utilization A (PutA).Archives of biochemistry and biophysics · 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
- Role of Proline in Pathogen and Host Interactions.Antioxidants & redox signaling · 2019Review
- Structural Biology of Proline Catabolic Enzymes.Antioxidants & redox signaling · 2019Review
- Redox Modulation of Oligomeric State in Proline Utilization A.Biophysical journal · 2018Article
- Functional Impact of the N-terminal Arm of Proline Dehydrogenase from Thermus thermophilus.Molecules (Basel, Switzerland) · 2018Article
- Structural Basis for the Substrate Inhibition of Proline Utilization A by Proline.Molecules (Basel, Switzerland) · 2017Article
- Article
- Structure, function, and mechanism of proline utilization A (PutA).Archives of biochemistry and biophysics · 2017Review
- Biophysical investigation of type A PutAs reveals a conserved core oligomeric structure.The FEBS journal · 2017Article
- Identification of a Conserved Histidine As Being Critical for the Catalytic Mechanism and Functional Switching of the Multifunctional Proline Utilization A Protein.Biochemistry · 2017Article
- Structure and characterization of a class 3B proline utilization A: Ligand-induced dimerization and importance of the C-terminal domain for catalysis.The Journal of biological chemistry · 2017Article
- Structures of Proline Utilization A (PutA) Reveal the Fold and Functions of the Aldehyde Dehydrogenase Superfamily Domain of Unknown Function.The Journal of biological chemistry · 2016Article
- First evidence for substrate channeling between proline catabolic enzymes: a validation of domain fusion analysis for predicting protein-protein interactions.The Journal of biological chemistry · 2015Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Proline utilization A from Bradyrhizobium japonicum (BjPutA) is a bifunctional flavoenzyme that catalyzes the oxidation of proline to glutamate using fused proline dehydrogenase (PRODH) and Δ(1)-pyrroline-5-carboxylate dehydrogenase (P5CDH) domains. Recent crystal structures and kinetic data suggest an intramolecular channel connects the two active sites, promoting substrate channeling of the intermediate Δ(1)-pyrroline-5-carboxylate/glutamate-γ-semialdehyde (P5C/GSA). In this work, the structure of the channel was explored by inserting large side chain residues at four positions along the channel in BjPutA. Kinetic analysis of the different mutants revealed replacement of D779 with Tyr (D779Y) or Trp (D779W) significantly decreased the overall rate of the PRODH-P5CDH channeling reaction. X-ray crystal structures of D779Y and D779W revealed that the large side chains caused a constriction in the central section of the tunnel, thus likely impeding the travel of P5C/GSA in the channel. The D779Y and D779W mutants have PRODH activity similar to that of wild-type BjPutA but exhibit significantly lower P5CDH activity, suggesting that exogenous P5C/GSA enters the channel upstream of Asp779. Replacement of nearby Asp778 with Tyr (D778Y) did not impact BjPutA channeling activity. Consistent with the kinetic results, the X-ray crystal structure of D778Y shows that the main channel pathway is not impacted; however, an off-cavity pathway is closed off from the channel. These findings provide evidence that the off-cavity pathway is not essential for substrate channeling in BjPutA.
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