This enzyme catalyses a step in a bacterial pathway for the biosynthesis of pyridoxal 5'-phosphate. The enzyme contains a tightly-bound NAD(H) cofactor that is not re-oxidized by free NAD+. In order to re-oxidize the cofactor and restore enzyme activity, the enzyme catalyses the reduction of a 2-oxo acid (such as 2-oxoglutarate, oxaloacetate, or pyruvate) to the respective (R)-hydroxy acid . cf. EC 1.1.1.399, 2-oxoglutarate reductase.
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SYSTEMATIC NAME
IUBMB Comments
4-phospho-D-erythronate:NAD+ 2-oxidoreductase
This enzyme catalyses a step in a bacterial pathway for the biosynthesis of pyridoxal 5'-phosphate. The enzyme contains a tightly-bound NAD(H) cofactor that is not re-oxidized by free NAD+. In order to re-oxidize the cofactor and restore enzyme activity, the enzyme catalyses the reduction of a 2-oxo acid (such as 2-oxoglutarate, oxaloacetate, or pyruvate) to the respective (R)-hydroxy acid [6]. cf. EC 1.1.1.399, 2-oxoglutarate reductase.
multiple turnovers requiring 2-oxo acids for re-oxidation of NADH bound to the enzyme PdxB a coupled assay with the enzymes SerC and PdxA following in the bioyntetic pathway, overview
the enzyme mediates a step in the biosynthesis of the coenzyme pyridoxal 5'-phosphate. Transcription of pdxB gene is positively growth rate regulated. PdxB-specific transcript remains unchanged during amino acid starvation in wild-type and relA mutant strains
the enzyme mediates a step in the biosynthesis of the coenzyme pyridoxal 5'-phosphate. Transcription of pdxB gene is positively growth rate regulated. PdxB-specific transcript remains unchanged during amino acid starvation in wild-type and relA mutant strains
pyridoxal phosphate biosynthesis in Escherichia coli is quite different from the more widely used Pdx1/Pdx2-dependent pathway. Escherichia coli uses seven enzymes in a bifurcated pathway that converts pyruvate, glyceraldehyde-3-phosphate, and erythrose-4-phosphate to pyridoxal phosphate via the intermediates 1-deoxy-D-xylulose 5-phosphate and 1-amino-propan-2-one-3-phosphate. PdxB catalyzes the second step in the biosynthesis of pyridoxal phosphate by oxidizing 4-phospho-D-erythronate to 2-oxo-3-hydroxy-4-phospho-butanoate with concomitant reduction
pyridoxal phosphate biosynthesis in Escherichia coli is quite different from the more widely used Pdx1/Pdx2-dependent pathway. Escherichia coli uses seven enzymes in a bifurcated pathway that converts pyruvate, glyceraldehyde-3-phosphate, and erythrose-4-phosphate to pyridoxal phosphate via the intermediates 1-deoxy-D-xylulose 5-phosphate and 1-amino-propan-2-one-3-phosphate. PdxB catalyzes the second step in the biosynthesis of pyridoxal phosphate by oxidizing 4-phospho-D-erythronate to 2-oxo-3-hydroxy-4-phospho-butanoate with concomitant reduction
the pdxB gene, encoding erythronate-4-phosphate dehydrogenase, is required for de novo vitamin B6 biosynthesis. Mutation in pdxB causes growth deficiency of Photorhabdus luminescens in nutrient-poor medium, which is restored under nutrient-rich conditions or by supplementation with pyridoxal 5'-phosphate. Supplementation with pyridoxal, pyridoxine, and pyridoxamine also restores the growth of the pdxB mutant. Supplementation with pyridoxal 5'-phosphate restores the virulence-deficient phenotype against Caenorhabditis elegans
the pdxB gene, encoding erythronate-4-phosphate dehydrogenase, is required for de novo vitamin B6 biosynthesis. Mutation in pdxB causes growth deficiency of Photorhabdus luminescens in nutrient-poor medium, which is restored under nutrient-rich conditions or by supplementation with pyridoxal 5'-phosphate. Supplementation with pyridoxal, pyridoxine, and pyridoxamine also restores the growth of the pdxB mutant. Supplementation with pyridoxal 5'-phosphate restores the virulence-deficient phenotype against Caenorhabditis elegans
homodimer, each subunit consists of three structural domains: the lid domain, the nucleotide-binding domain, and the C-terminal dimerization domain with a unique fold responsible for the dimerization, crystal structure analysis, overview
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging-drop vapour diffusion at 24°C K using 0.7 M ammonium dihydrogen phosphate, 0.4 M ammonium tartrate, 0.1 M sodium citrate pH 5.6 and 10 mM cupric chloride
purified recombinant C-terminally His8-tagged and selenomethionine-labeled enzyme, subunit A is bound with NAD+ and a phosphate ion, while subunit B, with a more open active site cleft, is bound with NAD+ and L(+)-tartrate, cryoprotection by 30% glycerol, X-ray diffraction structure determination and analysis at 2.3 A resolution, asymmetric subunit conformation and strucure comparison, overview