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Information on EC 1.1.1.290 - 4-phosphoerythronate dehydrogenase and Organism(s) Pseudomonas aeruginosa and UniProt Accession Q9I3W9

for references in articles please use BRENDA:EC1.1.1.290
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IUBMB 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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This record set is specific for:
Pseudomonas aeruginosa
UNIPROT: Q9I3W9
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Word Map
The taxonomic range for the selected organisms is: Pseudomonas aeruginosa
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
erythronate-4-phosphate dehydrogenase, 4-phosphoerythronate dehydrogenase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D-erythronate-4-phosphate dehydrogenase
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erythronate-4-phosphate dehydrogenase
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additional information
PdxB is a member of the D-isomer specific 2-hydroxyacid dehydrogenase superfamily
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
4-phospho-D-erythronate + NAD+ = (3R)-3-hydroxy-2-oxo-4-phosphooxybutanoate + NADH + H+
show the reaction diagram
substrate recognition and catalytic mechanism, PdxB contains the conserved His254/Glu237/Arg208 triad
PATHWAY SOURCE
PATHWAYS
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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.
CAS REGISTRY NUMBER
COMMENTARY hide
125858-75-5
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-phospho-D-erythronate + NAD+
(3R)-3-hydroxy-2-oxo-4-phosphooxybutanoate + NADH
show the reaction diagram
erythronate-4-phosphate + NAD+
3-hydroxy-4-phospho-hydroxy-alpha-ketobutyrate + NADH
show the reaction diagram
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-
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-
?
additional information
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
4-phospho-D-erythronate + NAD+
(3R)-3-hydroxy-2-oxo-4-phosphooxybutanoate + NADH
show the reaction diagram
the enzyme is involved in biosynthesis of pyridoxal-5'-phosphate
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-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NAD+
NAD+ is bound to the C-terminal side of the beta-sheet of the nucleotide-binding domain in both subunits of PdxB, binding structure, overview
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene pdxB
SwissProt
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
83000
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estimated by dynamic light-scattering analysis
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
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
homodimer
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2 * 42 067, enzyme including a C-terminal tag, enzyme consists of two identical 380-residue subunits
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
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
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
metal-chelate chromatography on Ni-NTA resin and size exclusion chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ha, J.Y.; Lee, J.H.; Kim, K.H.; Kim, D.J.; Lee, H.H.; Kim, H.K.; Yoon, H.J.; Suh, S.W.
Overexpression, crystallization and preliminary X-ray crystallographic analysis of erythronate-4-phosphate dehydrogenase from Pseudomonas aeruginosa
Acta Crystallogr. Sect. F
62
139-141
2006
Pseudomonas aeruginosa
Manually annotated by BRENDA team
Ha, J.Y.; Lee, J.H.; Kim, K.H.; Kim, d.o..J.; Lee, H.H.; Kim, H.K.; Yoon, H.J.; Suh, S.W.
Crystal structure of D-erythronate-4-phosphate dehydrogenase complexed with NAD
J. Mol. Biol.
366
1294-1304
2007
Pseudomonas aeruginosa (Q9I3W9), Pseudomonas aeruginosa
Manually annotated by BRENDA team