BRENDA - Enzyme Database
show all sequences of 1.1.1.262

Biosynthesis of vitamin B6: direct identification of the product of the PdxA-catalyzed oxidation of 4-hydroxy-L-threonine-4-phosphate using electrospray ionization mass spectrometry

Banks, J.; Cane, D.E.; Bioorg. Med. Chem. Lett. 14, 1633-16367 (2004)

Data extracted from this reference:

Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Zn2+
tightly bound, divalent metal ion-dependent enzyme, Zn2+ can be replaced by e.g. Mg2+
Escherichia coli
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
4-(phosphonooxy)threonine + NAD(P)+
Escherichia coli
involved in the biosynthesis of vitamin B6
3-amino-1-hydroxyacetone 1-phosphate + CO2 + NAD(P)H
-
-
?
Organism
Organism
UniProt
Commentary
Textmining
Escherichia coli
-
-
-
Reaction
Reaction
Commentary
Organism
Reaction ID
4-phosphooxy-L-threonine + NAD+ = 3-amino-2-oxopropyl phosphate + CO2 + NADH + H+
3-amino-1-hydroxyacetone 1-phosphate,i.e. AHAB, is the primary product of the reaction, no formation of 2-amino-3-oxo-4-phosphonooxybutyrate as intermediate is detected, identification by electrospray ionization mass spectrometry
Escherichia coli
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
4-(phosphonooxy)threonine + NAD(P)+
involved in the biosynthesis of vitamin B6
654972
Escherichia coli
3-amino-1-hydroxyacetone 1-phosphate + CO2 + NAD(P)H
-
-
-
?
4-(phosphonooxy)threonine + NAD(P)+
i.e. 4-hydroxy-L-threonine-4-phosphate, HTP
654972
Escherichia coli
3-amino-1-hydroxyacetone 1-phosphate + CO2 + NAD(P)H
i.e. AHAB, primary product of the reaction, no formation of 2-amino-3-oxo-4-phosphonooxybutyrate as intermediate is detected, identification by electrospray ionization mass spectrometry
-
-
?
Synonyms
Synonyms
Commentary
Organism
PdxA
-
Escherichia coli
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
-
assay at
Escherichia coli
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
assay at
Escherichia coli
Cofactor
Cofactor
Commentary
Organism
Structure
NAD(P)+
dependent on
Escherichia coli
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
NAD(P)+
dependent on
Escherichia coli
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Zn2+
tightly bound, divalent metal ion-dependent enzyme, Zn2+ can be replaced by e.g. Mg2+
Escherichia coli
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
ID
4-(phosphonooxy)threonine + NAD(P)+
Escherichia coli
involved in the biosynthesis of vitamin B6
3-amino-1-hydroxyacetone 1-phosphate + CO2 + NAD(P)H
-
-
?
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
4-(phosphonooxy)threonine + NAD(P)+
involved in the biosynthesis of vitamin B6
654972
Escherichia coli
3-amino-1-hydroxyacetone 1-phosphate + CO2 + NAD(P)H
-
-
-
?
4-(phosphonooxy)threonine + NAD(P)+
i.e. 4-hydroxy-L-threonine-4-phosphate, HTP
654972
Escherichia coli
3-amino-1-hydroxyacetone 1-phosphate + CO2 + NAD(P)H
i.e. AHAB, primary product of the reaction, no formation of 2-amino-3-oxo-4-phosphonooxybutyrate as intermediate is detected, identification by electrospray ionization mass spectrometry
-
-
?
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
-
assay at
Escherichia coli
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
-
assay at
Escherichia coli
Other publictions for EC 1.1.1.262
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
Synonyms
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)
654972
Banks
Biosynthesis of vitamin B6: di ...
Escherichia coli
Bioorg. Med. Chem. Lett.
14
1633-16367
2004
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656172
Sivaraman
Crystal structure of Escherich ...
Escherichia coli
J. Biol. Chem.
278
43682-43690
2003
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1
1
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3
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1
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207962
Laber
Vitamin B6 biosynthesis: forma ...
Escherichia coli
FEBS Lett.
449
45-48
1999
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207963
Cane
-
Biosynthesis of vitamin B6: en ...
Escherichia coli
J. Am. Chem. Soc.
121
7722-7723
1999
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1
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207964
Cane
-
Biosynthesis of vitamin B6: th ...
Escherichia coli
J. Am. Chem. Soc.
120
1936-1937
1998
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