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Enzyme Nomenclature
Information on EC 1.1.1.262 - 4-hydroxythreonine-4-phosphate dehydrogenase
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The expected taxonomic range for this enzyme is: Escherichia coli
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EC NUMBER 
COMMENTARY 
1.1.1.262
-
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RECOMMENDED NAME
GeneOntology No.
4-hydroxythreonine-4-phosphate dehydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
4-phosphooxy-L-threonine + NAD+ = 3-amino-2-oxopropyl phosphate + CO2 + NADH + H+
overall reaction
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-
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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
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
4-phosphooxy-L-threonine:NAD+ 3-oxidoreductase (decarboxylating)
The product of the reaction undergoes decarboxylation to give 3-amino-2-oxopropyl phosphate. The enzyme is part of the biosynthesis pathway of the coenzyme pyridoxal 5'-phosphate found in anaerobic bacteria.
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CAS REGISTRY NUMBER
COMMENTARY
230310-36-8
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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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
2-amino-3-oxo-4-phosphonooxybutyrate + H2O
3-amino-1-hydroxyacetone 1-phosphate + CO2
step 2 of the overall reaction
i.e. AHAP
-
?
4-(phosphohydroxy)-L-threonine + NAD+
3-phosphohydroxy-1aminoacetone + CO2 + NADH + H+
-
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
-
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
-
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
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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NATURAL SUBSTRATES
NATURAL PRODUCTS
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
4-(phosphohydroxy)-L-threonine + NAD+
3-phosphohydroxy-1aminoacetone + CO2 + NADH + H+
-
involved in pyridoxal 5'-phosphate formation
further condensation with 1-deoxy-D-xylulose-5-phosphate to form pyridoxal 5'-phosphate
r
4-(phosphonooxy)threonine + NAD(P)+
2-amino-3-oxo-4-phosphonooxybutyrate + NAD(P)H
P19624
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
-
involved in the biosynthesis of vitamin B6
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-
?
4-(phosphohydroxy)-L-threonine + NAD+
2-amino-3-oxo-4-phosphohydroxybutyrate + NADH
-
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
-
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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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Zn2+
Zn2+
-
tightly bound, divalent metal ion-dependent enzyme, Zn2+ can be replaced by e.g. Mg2+
Zn2+
divalent metal ion-dependent enzyme, Zn2+ is bound to the active site of each monomer coordinated by 3 histidine residues from both monomer
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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PDB
SCOP
CATH
ORGANISM
UNIPROT
Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168)
Paraburkholderia phymatum (strain DSM 17167 / CIP 108236 / LMG 21445 / STM815)
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
tightly bound, monomer fold is alpha/beta/alpha divided into 2 subdomains, the active site is located at the dimer interface
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography, cleavage by thrombin
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene pdxA, expression of the His-tagged enzyme with a thrombin cleavage site in Escherichia coli
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LINKS TO OTHER DATABASES (specific for EC-Number 1.1.1.262)
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