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Information on EC 1.1.1.290 - 4-phosphoerythronate dehydrogenase and Organism(s) Escherichia coli and UniProt Accession P05459
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1.1.1.290 4-phosphoerythronate dehydrogenaseIUBMB Comments
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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Word Map
- 1.1.1.290
-
2-hydroxyacid
- pyridoxine
-
salvage
- dehydrogenases
- aeruginosa
-
homodimeric
- pyridoxal
- 5'-phosphate
The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Reaction Schemes
Synonyms
erythronate-4-phosphate dehydrogenase, 4-phosphoerythronate dehydrogenase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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.
CAS REGISTRY NUMBER
COMMENTARY
125858-75-5
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
erythronate-4-phosphate + NAD+
(3R)-3-hydroxy-2-oxo-4-phosphonooxybutanoate + NADH
reaction in pathway leading from erythrose-4-phosphate and glutamate to nitrogen 1 and carbon 5,5', and 6 of the pyridoxine ring
-
-
?
2-oxoglutarate + NADH + H+
L-2-hydroxyglutarate + NAD+
-
stereospecific reaction
-
-
?
4-phospho-D-erythronate + NAD+
2-oxo-3-hydroxy-4-phospho-butanoate + NADH
-
-
-
-
?
4-phospho-D-erythronate + NAD+
2-oxo-3-hydroxy-4-phospho-butanoate + NADH + H+
-
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
-
-
?
4-phospho-D-erythronate + NAD+
3-hydroxy-2-oxo-4-(phosphonooxy)butanoate + NADH + H+
-
-
-
-
r
additional information
?
-
pdxB is the first gene in the pdxB-hisT operon
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
2,6-dichloroindolphenol, N-nitrosodimethylamine, and methylene blue cannot be reduced in the presence of the enzyme and 4-phospho-D-erythronate
-
-
?
additional information
?
-
-
2-oxoglutarate, oxaloacetic acid, and pyruvate are equally good subtrates for the enzyme
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
erythronate-4-phosphate + NAD+
(3R)-3-hydroxy-2-oxo-4-phosphonooxybutanoate + NADH
reaction in pathway leading from erythrose-4-phosphate and glutamate to nitrogen 1 and carbon 5,5', and 6 of the pyridoxine ring
-
-
?
4-phospho-D-erythronate + NAD+
2-oxo-3-hydroxy-4-phospho-butanoate + NADH
-
-
-
-
?
4-phospho-D-erythronate + NAD+
3-hydroxy-2-oxo-4-(phosphonooxy)butanoate + NADH + H+
-
-
-
-
r
additional information
?
-
pdxB is the first gene in the pdxB-hisT operon
-
-
?
additional information
?
-
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
-
-
?
additional information
?
-
-
2,6-dichloroindolphenol, N-nitrosodimethylamine, and methylene blue cannot be reduced in the presence of the enzyme and 4-phospho-D-erythronate
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
PdxB contains tightly bound NAD+ and/or NADH that cannot be removed by extensive dialysis
-
NADH
-
the enzyme contains a tightly bound NADH, the released cofactor is 10% NAD+ and 90% NADH
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
D-2-hydroxyglutarate
-
competitive versus 4-phospho-D-erythronate, noncompetitive versus 2-oxoglutarate
D-2-hydroxyglutaric acid
-
competitive inhibitor vs. 4-phospho-D-erythronate and a noncompetitive inhibitor vs. alpha-oxoglutarate
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.093
2-oxoglutarate
-
in 50 mM Tris-HCl (pH 8.0) with 50 mM NaCl, 1 mM dithiothreitol, at 22°C
0.086
oxaloacetic acid
-
in 50 mM Tris-HCl (pH 8.0) with 50 mM NaCl, 1 mM dithiothreitol, at 22°C
0.128
pyruvate
-
in 50 mM Tris-HCl (pH 8.0) with 50 mM NaCl, 1 mM dithiothreitol, at 22°C
0.0029
4-phospho-D-erythronate
-
in 50 mM Tris-HCl (pH 8.0) with 50 mM NaCl, 1 mM dithiothreitol, at 22°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1
2-oxoglutarate
-
in 50 mM Tris-HCl (pH 8.0) with 50 mM NaCl, 1 mM dithiothreitol, at 22°C
1.1
oxaloacetic acid
-
in 50 mM Tris-HCl (pH 8.0) with 50 mM NaCl, 1 mM dithiothreitol, at 22°C
1.3
pyruvate
-
in 50 mM Tris-HCl (pH 8.0) with 50 mM NaCl, 1 mM dithiothreitol, at 22°C
1.4
4-phospho-D-erythronate
-
in 50 mM Tris-HCl (pH 8.0) with 50 mM NaCl, 1 mM dithiothreitol, at 22°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
11
2-oxoglutarate
-
in 50 mM Tris-HCl (pH 8.0) with 50 mM NaCl, 1 mM dithiothreitol, at 22°C
13
oxaloacetic acid
-
in 50 mM Tris-HCl (pH 8.0) with 50 mM NaCl, 1 mM dithiothreitol, at 22°C
9.9
pyruvate
-
in 50 mM Tris-HCl (pH 8.0) with 50 mM NaCl, 1 mM dithiothreitol, at 22°C
6700
4-phospho-D-erythronate
-
in 50 mM Tris-HCl (pH 8.0) with 50 mM NaCl, 1 mM dithiothreitol, at 22°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.017
D-2-hydroxyglutarate
-
pH 8.0, 22°C, recombinant enzyme, versus 2-oxoglutarate
0.03
D-2-hydroxyglutarate
-
pH 8.0, 22°C, recombinant enzyme, versus 4-phospho-D-erythronate
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.102
D-2-hydroxyglutaric acid
Escherichia coli
-
in 50 mM Tris-HCl (pH 8.0) with 50 mM NaCl, 1 mM dithiothreitol, at 22°C
2
L-2-hydroxyglutaric acid
Escherichia coli
-
in 50 mM Tris-HCl (pH 8.0) with 50 mM NaCl, 1 mM dithiothreitol, at 22°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
-
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged PdxB from Escherichia coli stran BL21(DE3) by nickel affinity chromatography and ultrafiltration
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
coexpression of His-tagged PdxB, SerC, and PdxA in Escherichia coli stran BL21(DE3)
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Grant, G.A.
A new family of 2-hydroxyacid dehydrogenases
Biochem. Biophys. Res. Commun.
165
1371-1374
1989
Escherichia coli
Schoenlein, P.V.; Roa, B.B.; Winkler, M.E.
Divergent transcription of pdxB and homology between the pdxB and serA gene products in Escherichia coli K-12
J. Bacteriol.
171
6084-6092
1989
Escherichia coli (P05459)
Lam, H.M.; Winkler, M.E.
Metabolic relationships between pyridoxine (vitamin B6) and serine biosynthesis in Escherichia coli K-12
J. Bacteriol.
172
6518-6528
1990
Escherichia coli (P05459)
Pease, A.J.; Roa, B.R.; Luo, W.; Winkler, M.E.
Positive growth rate-dependent regulation of the pdxA, ksgA, and pdxB genes of Escherichia coli K-12
J. Bacteriol.
184
1359-1369
2002
Escherichia coli (P05459)
EXTERNAL LINKS (specific for EC-Number 1.1.1.290)
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