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EC Tree
IUBMB Comments A flavoprotein (FMN). In Escherichia coli, the coenzyme pyridoxal 5'-phosphate is synthesized de novo by a pathway that involves EC 1.2.1.72 (erythrose-4-phosphate dehydrogenase), EC 1.1.1.290 (4-phosphoerythronate dehydrogenase), EC 2.6.1.52 (phosphoserine transaminase), EC 1.1.1.262 (4-hydroxythreonine-4-phosphate dehydrogenase), EC 2.6.99.2 (pyridoxine 5'-phosphate synthase) and EC 1.4.3.5 (with pyridoxine 5'-phosphate as substrate). N4'-Substituted pyridoxamine derivatives are also oxidized in reaction (1) to form pyridoxal 5-phosphate and the corresponding primary amine.
The taxonomic range for the selected organisms is: Escherichia coli The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
pyridoxine 5'-phosphate oxidase, pnpox, pyridoxine phosphate oxidase, pyridox(am)ine 5'-phosphate oxidase, pnp oxidase, pyridoxine-5'-phosphate oxidase, pyridoxamine 5'-phosphate oxidase, pyridoxamine phosphate oxidase, pyridoxine (pyridoxamine) phosphate oxidase, pyridoxine (pyridoxamine) 5'-phosphate oxidase,
more
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pyridoxine 5'-phosphate oxidase
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pyridoxine 5-phosphate oxidase
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oxidase, pyridoxamine phosphate
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pyridoxamine 5'-phosphate oxidase
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pyridoxamine phosphate oxidase
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pyridoxamine-phosphate oxidase
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pyridoxaminephosphate oxidase (EC 1.4.3.5: deaminating)
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pyridoxine (pyridoxamine) 5'-phosphate oxidase
pyridoxine (pyridoxamine) phosphate oxidase
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pyridoxine 5'-phosphate oxidase
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PNPOx
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pyridoxine (pyridoxamine) 5'-phosphate oxidase
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pyridoxine (pyridoxamine) 5'-phosphate oxidase
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pyridoxamine 5'-phosphate + H2O + O2 = pyridoxal 5'-phosphate + NH3 + H2O2
pyridoxine 5'-phosphate + O2 = pyridoxal 5'-phosphate + H2O2
reaction mechanism, the oxidation involves a stereospecific hydride-ion transfer between C4' of pyridoxal 5'-phosphate and N5 of FMN, structure-function relationship, substrate binding and active site structure
pyridoxamine 5'-phosphate + H2O + O2 = pyridoxal 5'-phosphate + NH3 + H2O2
enzyme is specific for removal of the pro-R hydrogen atom from the prochiral C4' carbon atom of pyridoxamine 5'-phosphate, hydride ion mechanism is suggested
pyridoxamine 5'-phosphate + H2O + O2 = pyridoxal 5'-phosphate + NH3 + H2O2
reaction mechanism, the oxidation involves a stereospecific hydride-ion transfer between C4' of pyridoxal 5'-phosphate and N5 of FMN, structure-function relationship, substrate binding and active site structure
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pyridoxamine-5'-phosphate:oxygen oxidoreductase (deaminating)
A flavoprotein (FMN). In Escherichia coli, the coenzyme pyridoxal 5'-phosphate is synthesized de novo by a pathway that involves EC 1.2.1.72 (erythrose-4-phosphate dehydrogenase), EC 1.1.1.290 (4-phosphoerythronate dehydrogenase), EC 2.6.1.52 (phosphoserine transaminase), EC 1.1.1.262 (4-hydroxythreonine-4-phosphate dehydrogenase), EC 2.6.99.2 (pyridoxine 5'-phosphate synthase) and EC 1.4.3.5 (with pyridoxine 5'-phosphate as substrate). N4'-Substituted pyridoxamine derivatives are also oxidized in reaction (1) to form pyridoxal 5-phosphate and the corresponding primary amine.
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pyridoxamine 5'-phosphate + FMN + H2O + 2 H+
pyridoxal 5'-phosphate + FMNH2 + NH3
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-
-
?
pyridoxamine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + NH3 + H2O2
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-
?
pyridoxine 5'-phosphate + FMN
pyridoxal 5'-phosphate + FMNH2
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-
-
?
pyridoxine 5'-phosphate + O2
pyridoxal 5'-phosphate + H2O2
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-
-
?
pyridoxamine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + NH3 + H2O2
pyridoxine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + H2O2
pyridoxine 5'-phosphate + O2
pyridoxal 5'-phosphate + H2O2
pyridoxamine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + NH3 + H2O2
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-
-
?
pyridoxamine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + NH3 + H2O2
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-
-
?
pyridoxamine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + NH3 + H2O2
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-
-
?
pyridoxamine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + NH3 + H2O2
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-
-
?
pyridoxamine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + NH3 + H2O2
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-
-
-
?
pyridoxamine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + NH3 + H2O2
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terminal step in de novo biosynthesis of pyridoxal 5'-phosphate
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-
?
pyridoxamine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + NH3 + H2O2
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the enzyme prefers pyridoxine 5'-phosphate over pyridoxamine 5'-phosphate
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-
?
pyridoxine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + H2O2
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preferred substrate
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-
?
pyridoxine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + H2O2
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terminal step in de novo biosynthesis of pyridoxal 5'-phosphate
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-
?
pyridoxine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + H2O2
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the enzyme prefers pyridoxine 5'-phosphate over pyridoxamine 5'-phosphate
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-
?
pyridoxine 5'-phosphate + O2
pyridoxal 5'-phosphate + H2O2
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-
-
-
?
pyridoxine 5'-phosphate + O2
pyridoxal 5'-phosphate + H2O2
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the enzyme catalyzes the last step is pyridoxine 5'-phosphate oxidation to pyridoxal 5'-phosphate. The enzyme plays a pivotal role in controlling intracellular homeostasis and bioavailability of pyridoxal 5'-phosphate
-
-
?
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pyridoxamine 5'-phosphate + FMN + H2O + 2 H+
pyridoxal 5'-phosphate + FMNH2 + NH3
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-
-
?
pyridoxine 5'-phosphate + FMN
pyridoxal 5'-phosphate + FMNH2
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-
-
?
pyridoxine 5'-phosphate + O2
pyridoxal 5'-phosphate + H2O2
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-
-
?
pyridoxamine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + NH3 + H2O2
pyridoxine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + H2O2
pyridoxine 5'-phosphate + O2
pyridoxal 5'-phosphate + H2O2
pyridoxamine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + NH3 + H2O2
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?
pyridoxamine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + NH3 + H2O2
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terminal step in de novo biosynthesis of pyridoxal 5'-phosphate
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-
?
pyridoxine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + H2O2
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preferred substrate
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-
?
pyridoxine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + H2O2
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terminal step in de novo biosynthesis of pyridoxal 5'-phosphate
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-
?
pyridoxine 5'-phosphate + O2
pyridoxal 5'-phosphate + H2O2
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?
pyridoxine 5'-phosphate + O2
pyridoxal 5'-phosphate + H2O2
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the enzyme catalyzes the last step is pyridoxine 5'-phosphate oxidation to pyridoxal 5'-phosphate. The enzyme plays a pivotal role in controlling intracellular homeostasis and bioavailability of pyridoxal 5'-phosphate
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?
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FMN
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FMN
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FMN
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2 molecules of FMN bound per homodimer
FMN
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two molecules of FMN are noncovalently bound to the dimeric form of oxidase
FMN
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FMN-dependent enzyme
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pyridoxal 5'-phosphate
the enzyme undergoes an allosteric feedback inhibition by pyridoxal 5'-phosphate (PLP) caused by a strong allosteric coupling between PLP binding at the allosteric site and substrate binding at the active site. One PLP molecule is bound at the allosteric site of one monomer
4-deoxypyridoxine 5'-phosphate
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competitive inhibition
pyridoxine 5'-phosphate
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substrate inhibition
additional information
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pyridoxamine 5'-phosphate shows no substrate inhibition
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pyridoxal 5'-phosphate
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pyridoxal 5'-phosphate
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competitive inhibition
pyridoxal 5'-phosphate
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competitive inhibitor
pyridoxal 5'-phosphate
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product inhibition is of a mixed-type nature and results from binding of this vitamer at an allosteric site
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0.0003 - 2.4
pyridoxine 5'-phosphate
0.368
pyridoxal 5'-phosphate
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recombinant enzyme after cleavage from fusion protein
0.105 - 0.4
pyridoxamine 5'-phosphate
0.002 - 0.946
pyridoxine 5'-phosphate
additional information
additional information
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KM-values of mutant enzymes H199A, H199N, R197E, R197M, Y17F, R14E, R14M
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0.0003
pyridoxine 5'-phosphate
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0.0003
pyridoxine 5'-phosphate
H199N mutant enzyme
0.001
pyridoxine 5'-phosphate
D49A and Y17F mutant enzyme
0.0016
pyridoxine 5'-phosphate
pH 7.6, 37°C, wild-type enzyme
0.0017
pyridoxine 5'-phosphate
pH 7.6, 37°C, mutant enzyme R23L
0.002
pyridoxine 5'-phosphate
R14E mutant enzyme
0.0021
pyridoxine 5'-phosphate
pH 7.6, 37°C, mutant enzyme R23L/R24L
0.0024
pyridoxine 5'-phosphate
pH 7.6, 37°C, mutant enzyme K145A/F177A
0.0026
pyridoxine 5'-phosphate
R14M mutant enzyme
0.0026
pyridoxine 5'-phosphate
pH 7.6, 37°C, mutant enzyme R215L
0.0031
pyridoxine 5'-phosphate
pH 7.6, 37°C, mutant enzyme N84W/K145A/F177A
0.0032
pyridoxine 5'-phosphate
pH 7.6, 37°C, mutant enzyme N84A/K145A/F177A
0.0032
pyridoxine 5'-phosphate
pH 7.6, 37°C, mutant enzyme R23L/R215L
0.0034
pyridoxine 5'-phosphate
pH 7.6, 37°C, mutant enzyme R23L/R24L/R215L
0.07
pyridoxine 5'-phosphate
H199A mutant enzyme
0.09
pyridoxine 5'-phosphate
R197M mutant enzyme
2.4
pyridoxine 5'-phosphate
R197M mutant enzyme
0.105
pyridoxamine 5'-phosphate
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0.105
pyridoxamine 5'-phosphate
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recombinant enzyme
0.4
pyridoxamine 5'-phosphate
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recombinant enzyme after cleavage from fusion protein
0.002
pyridoxine 5'-phosphate
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0.002
pyridoxine 5'-phosphate
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recombinant enzyme
0.002
pyridoxine 5'-phosphate
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pH 8.5, 37°C
0.037
pyridoxine 5'-phosphate
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wild type enzyme, at pH 8.0 and 37°C
0.113
pyridoxine 5'-phosphate
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mutant enzyme K72P, at pH 8.0 and 37°C
0.219
pyridoxine 5'-phosphate
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mutant enzyme K72R, at pH 8.0 and 37°C
0.625
pyridoxine 5'-phosphate
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mutant enzyme K72A, at pH 8.0 and 37°C
0.946
pyridoxine 5'-phosphate
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mutant enzyme K72Q, at pH 8.0 and 37°C
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0.008 - 0.6
pyridoxine 5'-phosphate
33
pyridoxal 5'-phosphate
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recombinant enzyme after cleavage from fusion protein
1.72 - 28
pyridoxamine 5'-phosphate
0.0002 - 0.76
pyridoxine 5'-phosphate
additional information
additional information
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turnover numbers of mutant enzymes H199A, H199N, R197E, R197M, Y17F, R14E, R14M
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0.008
pyridoxine 5'-phosphate
R197M mutant enzyme
0.03
pyridoxine 5'-phosphate
H199N mutant enzyme
0.03
pyridoxine 5'-phosphate
R197M mutant enzyme
0.05
pyridoxine 5'-phosphate
pH 7.6, 37°C, mutant enzyme N84W/K145A/F177A
0.05
pyridoxine 5'-phosphate
pH 7.6, 37°C, mutant enzyme R215L
0.05
pyridoxine 5'-phosphate
pH 7.6, 37°C, mutant enzyme R23L/R215L
0.06
pyridoxine 5'-phosphate
D49A mutant enzyme
0.07
pyridoxine 5'-phosphate
pH 7.6, 37°C, mutant enzyme N84A/K145A/F177A
0.09
pyridoxine 5'-phosphate
pH 7.6, 37°C, mutant enzyme R23L
0.09
pyridoxine 5'-phosphate
pH 7.6, 37°C, mutant enzyme R23L/R24L/R215L
0.13
pyridoxine 5'-phosphate
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0.14
pyridoxine 5'-phosphate
H199A mutant enzyme
0.14
pyridoxine 5'-phosphate
R14M mutant enzyme
0.16
pyridoxine 5'-phosphate
R14E mutant enzyme
0.17
pyridoxine 5'-phosphate
pH 7.6, 37°C, mutant enzyme K145A/F177A
0.19
pyridoxine 5'-phosphate
pH 7.6, 37°C, mutant enzyme R23L-R24L
0.25
pyridoxine 5'-phosphate
pH 7.6, 37°C, wild-type enzyme
0.6
pyridoxine 5'-phosphate
Y17F mutant enzyme
1.72
pyridoxamine 5'-phosphate
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recombinant enzyme
28
pyridoxamine 5'-phosphate
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recombinant enzyme after cleavage from fusion protein
0.0002
pyridoxine 5'-phosphate
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mutant enzyme K72P, at pH 8.0 and 37°C
0.0004
pyridoxine 5'-phosphate
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mutant enzyme K72A, at pH 8.0 and 37°C
0.0015
pyridoxine 5'-phosphate
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mutant enzyme K72Q, at pH 8.0 and 37°C
0.022
pyridoxine 5'-phosphate
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wild type enzyme, at pH 8.0 and 37°C
0.024
pyridoxine 5'-phosphate
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mutant enzyme K72R, at pH 8.0 and 37°C
0.13
pyridoxine 5'-phosphate
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pH 8.5, 37°C
0.2
pyridoxine 5'-phosphate
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recombinant enzyme, in phosphate and HEPES buffer at pH 7.6
0.28
pyridoxine 5'-phosphate
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37°C, pH 7.6
0.3
pyridoxine 5'-phosphate
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recombinant enzyme, in Tris buffer at pH 7.6
0.76
pyridoxine 5'-phosphate
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recombinant enzyme
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0.105
4'-deoxypyridoxine-5'-phosphate
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-
0.008
pyridoxal 5'-phosphate
0.05
pyridoxine 5'-phosphate
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substrate inhibition
0.008
pyridoxal 5'-phosphate
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-
0.008
pyridoxal 5'-phosphate
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pH and temperature not specified in the publication
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0.000067
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activity in crude extracts, strain B
0.293
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recombinant enzyme
1.37
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recombinant enzyme
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8.3
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recombinant enzyme after cleavage from fusion protein
8.5
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pyridoxine phosphate oxidase activity, slight optimum
8.5 - 10
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pyridoxamine phosphate oxidase activity remains nearly constant between pH 8.5 and 10.0
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6 - 10
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pyridoxine phosphate oxidase activity
6.5 - 10
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pyridoxamine phosphate oxidase activity is absent at pH 6.0, rises sharply from pH 6.0 to 8.5 and remains constantly high between pH 8.5 and 10.0
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Uniprot
brenda
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metabolism
the enzyme is responsible for the last step of pyridoxal 5'-phosphate biosynthesis and is also involved in the pyridoxal 5'-phosphate salvage pathway
metabolism
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the enzyme catalyzes the last step is pyridoxine 5'-phosphate oxidation to pyridoxal 5'-phosphate. The enzyme plays a pivotal role in controlling intracellular homeostasis and bioavailability of pyridoxal 5'-phosphate
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25500
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recombinant enzyme after cleavage from fusion protein
28000
-
2 * 28000, SDS-PAGE
51000
-
-
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dimer
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2 * 28000, SDS-PAGE
monomer
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1 * 25500, recombinant enzyme after cleavage from fusion protein, gel filtration
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5 mg/ml purified native enzyme with FMN bound in 100 mM K2PO4, pH 7.5, and 5 mM 2-mercaptoethanol, mixed with an equal volume of reservoir solution containing 60 mM HEPES, pH 6.8, and 0.65 M KH2PO4/NH4H2PO4, formation of tetragonal crystals within 4-5 weeks, X-ray diffraction structure determination and analysis at 2.6 A resolution, molecular-replacement method
enzyme in complex with pyridoxal 5'-phosphate, space group C2, 2.07 A resolution
hanging drop vapor diffusion method
structures are defined at 2.0-2.1 A resolution
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D49A
decrease in affinity for pyridoxine 5'-phosphate
H199A
decrease in affinity for pyridoxine 5'-phosphate
H199N
little decrease in pyridoxine 5'-phosphate turnover
K145A/F177A
the Tm-value is about 1°C higher than the Tm-value of the wild-type enzyme
N84A/K145A/F177A
the Tm-value is about 3.3°C lower than the Tm-value of the wild-type enzyme
N84W/K145A/F177A
the Tm-value is about 3.4°C lower than the Tm-value of the wild-type enzyme
R14E
decrease in affinity for pyridoxine 5'-phosphate
R14M
decrease in affinity for pyridoxine 5'-phosphate
R197E
strong decrease in affinity for pyridoxine 5'-phosphate
R197M
catalyzes removal of the proS hydrogen atom from (4'R)-3H-pyridoxamine 5'-phosphate, decrease in affinity for pyridoxine 5'-phosphate
R215L
the Tm-value is 1°C lower than the Tm-value of the wild-type enzyme
R23L
the Tm-value is identical to the Tm-value of the wild-type enzyme
R23L/R215L
loosening of the allosteric coupling
R23L/R24L
loosening of the allosteric coupling
R23L/R24L/R21L
complete loss of allosteric properties. The Tm-value is about 2°C lower than the Tm-value of the wild-type enzyme
Y17F
decrease in affinity for pyridoxine 5'-phosphate
K159Q
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the mutation has no effect on the catalytic activity
K159R
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the mutation has no effect on the catalytic activity
K72A
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the mutant shows a sharp decrease of the catalytic activity compared to the wild type enzyme
K72P
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the mutant shows a sharp decrease of the catalytic activity compared to the wild type enzyme
K72Q
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the mutant shows a sharp decrease of the catalytic activity compared to the wild type enzyme
K72R
-
the mutant shows a slight decrease of the catalytic activity compared to the wild type enzyme
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66.6
Tm-value, mutant enzyme N84W/K145A/F177A
66.7
Tm-value, mutant enzyme N84A/K145A/F177A
68
Tm-value, mutant enzyme R23L/R24L/R215L
68.9
Tm-value, mutant enzyme R23L/R215L
69
Tm-value, mutant enzyme R215L
70.9
Tm-value, mutant enzyme K145A/F177A
71.1
Tm-value, mutant enzyme R23L/R24L
65
-
no loss in activity after incubation at temperatures below 50°C, 30% to 40% activity loss after 15 min at 65°C
70
Tm-value, wild-type enzyme
70
Tm-value, mutant enzyme R23L
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acetylation leads to a decrease of the enzymatic activity
-
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-75°C, 15% glycerol, several months, no loss in activity
-
4°C, several weeks, no loss of activity
-
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native enzyme with tightly bound FMN
nickel affinity column chromatography
-
recombinant enzyme, DEAE-cellulose, hydroxyapatite, CM-cellulose, Bio-Gel
-
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wild-type and mutant enzyme
expressed in Escherichia coli BL21(DE3) cells
-
expression in Escherichia coli
-
expression in Escherichia coli as maltose binding protein fusion
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expression in Escherichia coli MDS00 strain cells lacking pdxH gene
-
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Pflug, W.; Lingens, F.
Occurrence of pydixaminephosphate oxidase and pyridoxal kinase in Gram-negative and Gram-positive bacteria
Hoppe-Seyler's Z. Physiol. Chem.
364
1627-1630
1983
Agrobacterium tumefaciens, Chloridazon-degrading bacterium, Deinococcus radiodurans, Escherichia coli, Flavobacterium sp., Flavobacterium sp. CB6, no activity in Arthrobacter globiformis, no activity in Arthrobacter sp., no activity in Arthrobacter sp. SuC 3, no activity in Bacillus cereus, no activity in Bacillus circulans, no activity in Bacillus pasteurii, no activity in Bacillus polymyxa, no activity in Bacillus subtilis, no activity in Micrococcus luteus, no activity in Nocardia sp., no activity in Nocardia sp. CBS 2, Proteus mirabilis, Pseudomonas chlororaphis subsp. aureofaciens, Pseudomonas fluorescens, Pseudomonas putida, Pseudomonas sp., Pseudomonas sp. CBS 4, Rhodospirillum rubrum, Salmonella enterica subsp. enterica serovar Typhimurium, Serratia marcescens, Xanthomonas sp.
brenda
Zhao, G.; Winkler, M.E.
Kinetic limitation and cellular amount of pyridoxine (pyridoxamine) 5'-phosphate oxidase of Escherichia coli K-12
J. Bacteriol.
177
883-891
1995
Escherichia coli
brenda
Notheis, C.; Drewke, C.; Leistner, E.
Purification and characterization of the pyridoxol-5'-phosphate:oxygen oxidoreductase (deaminating) from Escherichia coli
Biochim. Biophys. Acta
1247
265-271
1995
Escherichia coli
brenda
Di Salvo, M.; Yang, E.; Zhao, G.; Winkler, M.E.; Schirch, V.
Expression, purification, and characterization of recombinant Escherichia coli pyridoxine 5'-phosphate oxidase
Protein Expr. Purif.
13
349-356
1998
Escherichia coli
brenda
Di Salvo, M.L.; Ko, T.P.; Musayev, F.N.; Raboni, S.; Schirch, V.; Safo, M.K.
Active site structure and stereospecificity of Escherichia coli pyridoxine-5'-phosphate oxidase
J. Mol. Biol.
315
385-397
2002
Escherichia coli (P0AFI7), Escherichia coli
brenda
di Salvo, M.L.; Safo, M.K.; Musayev, F.N.; Bossa, F.; Schirch, V.
Structure and mechanism of Escherichia coli pyridoxine 5'-phosphate oxidase
Biochim. Biophys. Acta
1647
76-82
2003
Escherichia coli
brenda
Safo, M.K.; Musayev, F.N.; Schirch, V.
Structure of Escherichia coli pyridoxine 5-phosphate oxidase in a tetragonal crystal form: insights into the mechanistic pathway of the enzyme
Acta Crystallogr. Sect. D
61
599-604
2005
Escherichia coli (P0AFI7), Escherichia coli
brenda
di Salvo, M.L.; Contestabile, R.; Safo, M.K.
Vitamin B6 salvage enzymes: mechanism, structure and regulation
Biochim. Biophys. Acta
1814
1597-1608
2011
Escherichia coli, Homo sapiens
brenda
Gu, J.; Chen, Y.; Guo, H.; Sun, M.; Yang, M.; Wang, X.; Zhang, X.; Deng, J.
Lysine acetylation regulates the activity of Escherichia coli pyridoxine 5'-phosphate oxidase
Acta Biochim. Biophys. Sin.
49
186-192
2017
Escherichia coli
brenda
Barile, A.; Tramonti, A.; di Salvo, M.L.; Nogues, I.; Nardella, C.; Malatesta, F.; Contestabile, R.
Allosteric feedback inhibition of pyridoxine 5-phosphate oxidase from Escherichia coli
J. Biol. Chem.
294
15593-15603
2019
Escherichia coli
brenda
Barile, A.; Battista, T.; Fiorillo, A.; di Salvo, M.; Malatesta, F.; Tramonti, A.; Ilari, A.; Contestabile, R.
Identification and characterization of the pyridoxal 5-phosphate allosteric site in Escherichia coli pyridoxine 5-phosphate oxidase
J. Biol. Chem.
296
100795
2021
Escherichia coli (P0AFI7), Escherichia coli, Escherichia coli K12 (P0AFI7)
brenda
Transporter Classification Database (TCDB):
2.A.7.2.4