ArticleThe Journal of biological chemistry2015
First evidence for substrate channeling between proline catabolic enzymes: a validation of domain fusion analysis for predicting protein-protein interactions.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 42 citations in OpenAlex.
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- Multiple Functions of Compatible Solute Ectoine and Strategies for Constructing Overproducers for Biobased Production.Molecular biotechnology · 2024Review
- Evidence of isochorismate channeling between the Escherichia coli enterobactin biosynthetic enzymes EntC and EntB.Protein science : a publication of the Protein Society · 2024Article
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- Proline Dehydrogenase and Pyrroline 5 Carboxylate Dehydrogenase fromPathogens (Basel, Switzerland) · 2023Article
- Proline utilization A controls bacterial pathogenicity by sensing its substrate and cofactors.Communications biology · 2022Article
- Research progress and the biotechnological applications of multienzyme complex.Applied microbiology and biotechnology · 2021Review
- Nuclear metabolism and the regulation of the epigenome.Nature metabolism · 2020Review
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- Engineering of Metabolic Pathways Using Synthetic Enzyme Complexes.Plant physiology · 2019Review
- Structural Biology of Proline Catabolic Enzymes.Antioxidants & redox signaling · 2019Review
- Proline Metabolism in Cell Regulation and Cancer Biology: Recent Advances and Hypotheses.Antioxidants & redox signaling · 2019Review
- Role of Proline in Pathogen and Host Interactions.Antioxidants & redox signaling · 2019Review
- Can enzyme proximity accelerate cascade reactions?Scientific reports · 2019Article
- The role of dynamic enzyme assemblies and substrate channelling in metabolic regulation.Nature communications · 2018Review
- Functional Impact of the N-terminal Arm of Proline Dehydrogenase from Thermus thermophilus.Molecules (Basel, Switzerland) · 2018Article
- Article
- Structure, function, and mechanism of proline utilization A (PutA).Archives of biochemistry and biophysics · 2017Review
- 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
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Proline dehydrogenase (PRODH) and Δ(1)-pyrroline-5-carboxylate (P5C) dehydrogenase (P5CDH) catalyze the four-electron oxidation of proline to glutamate via the intermediates P5C and l-glutamate-γ-semialdehyde (GSA). In Gram-negative bacteria, PRODH and P5CDH are fused together in the bifunctional enzyme proline utilization A (PutA) whereas in other organisms PRODH and P5CDH are expressed as separate monofunctional enzymes. Substrate channeling has previously been shown for bifunctional PutAs, but whether the monofunctional enzymes utilize an analogous channeling mechanism has not been examined. Here, we report the first evidence of substrate channeling in a PRODH-P5CDH two-enzyme pair. Kinetic data for the coupled reaction of PRODH and P5CDH from Thermus thermophilus are consistent with a substrate channeling mechanism, as the approach to steady-state formation of NADH does not fit a non-channeling two-enzyme model. Furthermore, inactive P5CDH and PRODH mutants inhibit NADH production and increase trapping of the P5C intermediate in coupled assays of wild-type PRODH-P5CDH enzyme pairs, indicating that the mutants disrupt PRODH-P5CDH channeling interactions. A dissociation constant of 3 μm was estimated for a putative PRODH-P5CDH complex by surface plasmon resonance (SPR). Interestingly, P5CDH binding to PRODH was only observed when PRODH was immobilized with the top face of its (βα)8 barrel exposed. Using the known x-ray crystal structures of PRODH and P5CDH from T. thermophilus, a model was built for a proposed PRODH-P5CDH enzyme channeling complex. The structural model predicts that the core channeling pathway of bifunctional PutA enzymes is conserved in monofunctional PRODH-P5CDH enzyme pairs.
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