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EC Tree
IUBMB Comments The enzyme is part of the biosynthesis pathway of the coenzyme pyridoxal 5'-phosphate found in anaerobic bacteria.
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
4-(phosphohydroxy)-L-threonine dehydrogenase, L-threonine 4-phosphate dehydrogenase, NAD-dependent threonine 4-phosphate dehydrogenase, PdxA,
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4-(phosphohydroxy)-L-threonine dehydrogenase
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L-threonine 4-phosphate dehydrogenase
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NAD-dependent threonine 4-phosphate dehydrogenase
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PdxA
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4-phosphooxy-L-threonine + NAD+ = 3-amino-2-oxopropyl phosphate + CO2 + NADH + H+
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
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4-phosphooxy-L-threonine + NAD+ = 3-amino-2-oxopropyl phosphate + CO2 + NADH + H+
Asp247 and Asp267 are involved in formation and maintaining of the integrity of the active site
4-phosphooxy-L-threonine + NAD+ = 3-amino-2-oxopropyl phosphate + CO2 + NADH + H+
overall reaction
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4-phosphooxy-L-threonine:NAD+ 3-oxidoreductase (decarboxylating)
The enzyme is part of the biosynthesis pathway of the coenzyme pyridoxal 5'-phosphate found in anaerobic bacteria.
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2-amino-3-oxo-4-phosphonooxybutyrate + H2O
3-amino-1-hydroxyacetone 1-phosphate + CO2
step 2 of the overall reaction
i.e. AHAP
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4-(phosphohydroxy)-L-threonine + NAD+
2-amino-3-oxo-4-phosphohydroxybutyrate + NADH
4-(phosphohydroxy)-L-threonine + NAD+
3-phosphohydroxy-1aminoacetone + CO2 + NADH + H+
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involved in pyridoxal 5'-phosphate formation
further condensation with 1-deoxy-D-xylulose-5-phosphate to form pyridoxal 5'-phosphate
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4-(phosphonooxy)threonine + NAD(P)+
2-amino-3-oxo-4-phosphonooxybutyrate + NAD(P)H
4-(phosphonooxy)threonine + NAD(P)+
3-amino-1-hydroxyacetone 1-phosphate + CO2 + NAD(P)H
4-(phosphohydroxy)-L-threonine + NAD+
2-amino-3-oxo-4-phosphohydroxybutyrate + NADH
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involved in pyridoxal 5'-phosphate formation
further condensation with 1-deoxy-D-xylulose-5-phosphate to form pyridoxal 5'-phosphate
r
4-(phosphohydroxy)-L-threonine + NAD+
2-amino-3-oxo-4-phosphohydroxybutyrate + NADH
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involved in pyridoxal 5'-phosphate formation
undergoes decarboxylation either catalysed by the enzyme or after release, further formation of pyridoxal 5'-phosphate catalysed by PdxJ protein
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4-(phosphonooxy)threonine + NAD(P)+
2-amino-3-oxo-4-phosphonooxybutyrate + NAD(P)H
fourth step of the pyridoxal 5'-phosphate biosynthesis
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4-(phosphonooxy)threonine + NAD(P)+
2-amino-3-oxo-4-phosphonooxybutyrate + NAD(P)H
i.e. 4-hydroxy-L-threonine phosphate or HTP, enzyme strictly requires the phosphate ester form of the substrate, interaction between enzyme and substrate via phosphate group, step 1 of the overall reaction
reaction intermediate
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4-(phosphonooxy)threonine + NAD(P)+
3-amino-1-hydroxyacetone 1-phosphate + CO2 + NAD(P)H
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involved in the biosynthesis of vitamin B6
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4-(phosphonooxy)threonine + NAD(P)+
3-amino-1-hydroxyacetone 1-phosphate + CO2 + NAD(P)H
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i.e. 4-hydroxy-L-threonine-4-phosphate, HTP
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
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4-(phosphohydroxy)-L-threonine + NAD+
2-amino-3-oxo-4-phosphohydroxybutyrate + NADH
4-(phosphohydroxy)-L-threonine + NAD+
3-phosphohydroxy-1aminoacetone + CO2 + NADH + H+
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involved in pyridoxal 5'-phosphate formation
further condensation with 1-deoxy-D-xylulose-5-phosphate to form pyridoxal 5'-phosphate
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4-(phosphonooxy)threonine + NAD(P)+
2-amino-3-oxo-4-phosphonooxybutyrate + NAD(P)H
fourth step of the pyridoxal 5'-phosphate biosynthesis
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4-(phosphonooxy)threonine + NAD(P)+
3-amino-1-hydroxyacetone 1-phosphate + CO2 + NAD(P)H
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involved in the biosynthesis of vitamin B6
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4-(phosphohydroxy)-L-threonine + NAD+
2-amino-3-oxo-4-phosphohydroxybutyrate + NADH
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involved in pyridoxal 5'-phosphate formation
further condensation with 1-deoxy-D-xylulose-5-phosphate to form pyridoxal 5'-phosphate
r
4-(phosphohydroxy)-L-threonine + NAD+
2-amino-3-oxo-4-phosphohydroxybutyrate + NADH
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involved in pyridoxal 5'-phosphate formation
undergoes decarboxylation either catalysed by the enzyme or after release, further formation of pyridoxal 5'-phosphate catalysed by PdxJ protein
r
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NAD(P)+
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dependent on
NAD(P)+
putative binding site structure
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Zn2+
divalent metal ion-dependent enzyme, Zn2+ is bound to the active site of each monomer coordinated by 3 histidine residues from both monomer
Zn2+
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tightly bound, divalent metal ion-dependent enzyme, Zn2+ can be replaced by e.g. Mg2+
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EDTA
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inhibition at 1 mM, fully restored by addition of 1 mM Mn2+, Co2+, Mg2+ or Ca2+, partially restored by 1 mM Ni2+ or Zn2+
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1.4
4-(phosphohydroxy)-L-threonine
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Uniprot
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additional information
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pdxA gene product
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additional information
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pdxA gene product
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additional information
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pdxA gene product
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dimer
tightly bound, monomer fold is alpha/beta/alpha divided into 2 subdomains, the active site is located at the dimer interface
monomer
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gel filtration, native PAGE, SDS-PAGE
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8.1 mg/ml purified recombinant enzyme in complex with substrate 4-(phosphonooxy)threonine and Zn2+ in 20 mM Tris-HCl, pH 8.0, 0.2 M NaCl, 10 mM DTT, 5% w/v glycerol, hanging drop vapour diffusion method, 0.002 ml protein solution with 0.004 ml reservoir solution, usage of 2 reservoir solution variants resulting in 2 differen crystal forms, solution 1 contains 7.5% w/v PEG 8000, 0.1 M NaOAc, pH 5.5, 10 mM MgCl2, 10 mM NaKHPO4, pH 5.9, solution 2 contains 20% w/v PEG 8000, 100 mM HEPES, pH 7.5, 75 mM citrate, and 100 mM MgCl2, suspension over reservoir solution, X-ray diffraction structure determination and analysis at 2,0 and 2.45 A resolution, respectively
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recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography, cleavage by thrombin
to homogeneity, recombinant enzyme
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gene pdxA, expression of the His-tagged enzyme with a thrombin cleavage site in Escherichia coli
overexpression in Escherichia coli
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Laber, B.; Maurer, W.; Scharf, S.; Stepusin, K.; Schmidt, F.S.
Vitamin B6 biosynthesis: formation of pyridoxine 5'-phosphate from 4-(phosphohydroxy)-L-threonine and 1-deoxy-D-xylulose-5-phosphate by PdxA and PdxJ protein
FEBS Lett.
449
45-48
1999
Escherichia coli
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Cane, D.E.; Du, S.; Robinson, J.K.; Hsiung, Y.; Spenser, I.D.
Biosynthesis of vitamin B6: enzymatic conversion of 1-deoxy-D-xylulose-5-phosphate to pyridoxol phosphate
J. Am. Chem. Soc.
121
7722-7723
1999
Escherichia coli
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Cane, D.E.; Hsiung, Y.; Cornish, J.A.; Robinson, J.K.; Spenser, I.D.
Biosynthesis of vitamin B6: the oxidation of 4-(phosphohydroxy)-L-threonine by PdxA
J. Am. Chem. Soc.
120
1936-1937
1998
Escherichia coli
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Banks, J.; Cane, D.E.
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
Bioorg. Med. Chem. Lett.
14
1633-16367
2004
Escherichia coli
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Sivaraman, J.; Li, Y.; Banks, J.; Cane, D.E.; Matte, A.; Cygler, M.
Crystal structure of Escherichia coli PdxA, an enzyme involved in the pyridoxal phosphate biosynthesis pathway
J. Biol. Chem.
278
43682-43690
2003
Escherichia coli (P19624), Escherichia coli
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1.1.1.262 4-hydroxythreonine-4-phosphate dehydrogenase
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