ArticleBiochemistry2010
Multiple turnovers of the nicotino-enzyme PdxB require α-keto acids as cosubstrates.
Article in Biochemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 25 citations in OpenAlex.
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- Functional Characterization of Cj1427, a Unique Ping-Pong Dehydrogenase Responsible for the Oxidation of GDP-d-Biochemistry · 2020Article
- Structural Analysis of Cj1427, an Essential NAD-Dependent Dehydrogenase for the Biosynthesis of the Heptose Residues in the Capsular Polysaccharides ofBiochemistry · 2020Article
- Relation of theInternational journal of molecular sciences · 2019Article
- A Survey of Pyridoxal 5'-Phosphate-Dependent Proteins in the Gram-Positive Model BacteriumFrontiers in molecular biosciences · 2019Review
- Classification, substrate specificity and structural features of D-2-hydroxyacid dehydrogenases: 2HADH knowledgebase.BMC evolutionary biology · 2018Article
- d-2-Hydroxyglutarate dehydrogenase plays a dual role in l-serine biosynthesis and d-malate utilization in the bacteriumThe Journal of biological chemistry · 2018Article
- Coupling between d-3-phosphoglycerate dehydrogenase and d-2-hydroxyglutarate dehydrogenase drives bacterial l-serine synthesis.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Mycofactocin-associated mycobacterial dehydrogenases with non-exchangeable NAD cofactors.Scientific reports · 2017Article
- Saccharomyces cerevisiae Forms D-2-Hydroxyglutarate and Couples Its Degradation to D-Lactate Formation via a Cytosolic Transhydrogenase.The Journal of biological chemistry · 2016Article
- Inhibitory cross-talk upon introduction of a new metabolic pathway into an existing metabolic network.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- A Simple Route for Synthesis of 4-Phospho-D-Erythronate.Tetrahedron letters · 2011Article
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Authors and funding
3 authors at 3 institutions in 2 countries.
Funding
Abstract
PdxB catalyzes the second step in the biosynthesis of pyridoxal phosphate by oxidizing 4-phospho-d-erythronate (4PE) to 2-oxo-3-hydroxy-4-phosphobutanoate (OHPB) with concomitant reduction of NAD(+) to NADH. PdxB is a nicotino-enzyme wherein the NAD(H) cofactor remains tightly bound to PdxB. It has been a mystery how PdxB performs multiple turnovers since addition of free NAD(+) does not reoxidize the enzyme-bound NADH following conversion of 4PE to OHPB. We have solved this mystery by demonstrating that a variety of physiologically available α-keto acids serve as oxidants of PdxB to sustain multiple turnovers. In a coupled assay using the next two enzymes of the biosynthetic pathway for pyridoxal phosphate (SerC and PdxA), we have found that α-ketoglutarate, oxaloacetic acid, and pyruvate are equally good substrates for PdxB (k(cat)/K(m) values ~1 × 10(4) M⁻¹s⁻¹). The kinetic parameters for the substrate 4PE include a k(cat) of 1.4 s⁻¹, a K(m) of 2.9 μM, and a k(cat)/K(m) of 6.7 × 10(6) M⁻¹s⁻¹. Additionally, we have characterized the stereochemistry of α-ketoglutarate reduction by showing that d-2-HGA, but not l-2-HGA, is a competitive inhibitor vs 4PE and a noncompetitive inhibitor vs α-ketoglutarate.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.