BRENDA - Enzyme Database
show all sequences of 1.1.1.290

Crystal structure of D-erythronate-4-phosphate dehydrogenase complexed with NAD

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.; J. Mol. Biol. 366, 1294-1304 (2007)

Data extracted from this reference:

Crystallization (Commentary)
Crystallization
Organism
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
Pseudomonas aeruginosa
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
4-phospho-D-erythronate + NAD+
Pseudomonas aeruginosa
the enzyme is involved in biosynthesis of pyridoxal-5'-phosphate
(3R)-3-hydroxy-2-oxo-4-phosphooxybutanoate + NADH
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Pseudomonas aeruginosa
Q9I3W9
gene pdxB
-
Reaction
Reaction
Commentary
Organism
4-phospho-D-erythronate + NAD+ = (3R)-3-hydroxy-2-oxo-4-phosphooxybutanoate + NADH + H+
substrate recognition and catalytic mechanism, PdxB contains the conserved His254/Glu237/Arg208 triad
Pseudomonas aeruginosa
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
4-phospho-D-erythronate + NAD+
-
688340
Pseudomonas aeruginosa
(3R)-3-hydroxy-2-oxo-4-phosphooxybutanoate + NADH
-
-
-
?
4-phospho-D-erythronate + NAD+
the enzyme is involved in biosynthesis of pyridoxal-5'-phosphate
688340
Pseudomonas aeruginosa
(3R)-3-hydroxy-2-oxo-4-phosphooxybutanoate + NADH
-
-
-
?
additional information
active site and ligand binding structure, overview
688340
Pseudomonas aeruginosa
?
-
-
-
-
Subunits
Subunits
Commentary
Organism
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
Pseudomonas aeruginosa
Cofactor
Cofactor
Commentary
Organism
Structure
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
Pseudomonas aeruginosa
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
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
Pseudomonas aeruginosa
Crystallization (Commentary) (protein specific)
Crystallization
Organism
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
Pseudomonas aeruginosa
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
4-phospho-D-erythronate + NAD+
Pseudomonas aeruginosa
the enzyme is involved in biosynthesis of pyridoxal-5'-phosphate
(3R)-3-hydroxy-2-oxo-4-phosphooxybutanoate + NADH
-
-
?
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
4-phospho-D-erythronate + NAD+
-
688340
Pseudomonas aeruginosa
(3R)-3-hydroxy-2-oxo-4-phosphooxybutanoate + NADH
-
-
-
?
4-phospho-D-erythronate + NAD+
the enzyme is involved in biosynthesis of pyridoxal-5'-phosphate
688340
Pseudomonas aeruginosa
(3R)-3-hydroxy-2-oxo-4-phosphooxybutanoate + NADH
-
-
-
?
additional information
active site and ligand binding structure, overview
688340
Pseudomonas aeruginosa
?
-
-
-
-
Subunits (protein specific)
Subunits
Commentary
Organism
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
Pseudomonas aeruginosa
Other publictions for EC 1.1.1.290
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
739912
Sato
Involvement of vitamin B6 bios ...
Photorhabdus luminescens, Photorhabdus luminescens DSM 15139
Appl. Environ. Microbiol.
82
3546-3553
2016
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724295
Rudolph
Multiple turnovers of the nico ...
Escherichia coli, Escherichia coli JW2317
Biochemistry
49
9249-9255
2010
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4
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2
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4
688340
Ha
Crystal structure of D-erythro ...
Pseudomonas aeruginosa
J. Mol. Biol.
366
1294-1304
2007
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667077
Ha
Overexpression, crystallizatio ...
Pseudomonas aeruginosa
Acta Crystallogr. Sect. F
62
139-141
2006
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1
1
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1
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3
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1
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1
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1
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661998
Pease
Positive growth rate-dependent ...
Escherichia coli
J. Bacteriol.
184
1359-1369
2002
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661981
Lam
Metabolic relationships betwee ...
Escherichia coli
J. Bacteriol.
172
6518-6528
1990
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660846
Grant
A new family of 2-hydroxyacid ...
Escherichia coli
Biochem. Biophys. Res. Commun.
165
1371-1374
1989
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661979
Schoenlein
Divergent transcription of pdx ...
Escherichia coli
J. Bacteriol.
171
6084-6092
1989
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