Any feedback?
Information on EC 1.4.3.5 - pyridoxal 5'-phosphate synthase and Organism(s) Escherichia coli and UniProt Accession P0AFI7
for references in articles please use BRENDA:EC1.4.3.5Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
1.4.3.5 pyridoxal 5'-phosphate synthaseIUBMB 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.
Specify your search results
Word Map
The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
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
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
FprA protein
-
-
-
-
oxidase, pyridoxamine phosphate
-
-
-
-
PMP oxidase
-
-
-
-
PNP/PMP oxidase
-
-
-
-
PNPOx
pyridoxamine 5'-phosphate oxidase
-
-
-
-
pyridoxamine phosphate oxidase
-
-
-
-
pyridoxamine-phosphate oxidase
-
-
-
-
pyridoxaminephosphate oxidase (EC 1.4.3.5: deaminating)
-
-
-
-
pyridoxine (pyridoxamine) 5'-phosphate oxidase
pyridoxine (pyridoxamine) phosphate oxidase
-
-
-
-
PNPOx
-
-
-
-
pyridoxine (pyridoxamine) 5'-phosphate oxidase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Deamination
-
-
-
-
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-, -, -, -
SYSTEMATIC NAME
IUBMB Comments
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.
CAS REGISTRY NUMBER
COMMENTARY
9029-21-4
-
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
pyridoxamine 5'-phosphate + FMN + H2O + 2 H+
pyridoxal 5'-phosphate + FMNH2 + NH3
-
-
-
?
pyridoxamine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + NH3 + H2O2
-
-
?
pyridoxamine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + NH3 + H2O2
-
-
-
?
pyridoxamine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + NH3 + H2O2
-
-
-
?
pyridoxamine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + NH3 + H2O2
-
-
-
?
pyridoxamine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + NH3 + H2O2
-
-
-
?
pyridoxamine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + NH3 + H2O2
-
-
-
-
?
pyridoxamine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + NH3 + H2O2
-
terminal step in de novo biosynthesis of pyridoxal 5'-phosphate
-
-
?
pyridoxamine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + NH3 + H2O2
-
the enzyme prefers pyridoxine 5'-phosphate over pyridoxamine 5'-phosphate
-
-
?
pyridoxine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + H2O2
-
preferred substrate
-
-
?
pyridoxine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + H2O2
-
terminal step in de novo biosynthesis of pyridoxal 5'-phosphate
-
-
?
pyridoxine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + H2O2
-
the enzyme prefers pyridoxine 5'-phosphate over pyridoxamine 5'-phosphate
-
-
?
pyridoxine 5'-phosphate + O2
pyridoxal 5'-phosphate + H2O2
-
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
-
-
?
NATURAL SUBSTRATE
NATURAL 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
pyridoxamine 5'-phosphate + FMN + H2O + 2 H+
pyridoxal 5'-phosphate + FMNH2 + NH3
-
-
-
?
pyridoxamine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + NH3 + H2O2
-
-
-
-
?
pyridoxamine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + NH3 + H2O2
-
terminal step in de novo biosynthesis of pyridoxal 5'-phosphate
-
-
?
pyridoxine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + H2O2
-
preferred substrate
-
-
?
pyridoxine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + H2O2
-
terminal step in de novo biosynthesis of pyridoxal 5'-phosphate
-
-
?
pyridoxine 5'-phosphate + O2
pyridoxal 5'-phosphate + H2O2
-
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
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FMN
-
two molecules of FMN are noncovalently bound to the dimeric form of oxidase
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
additional information
-
pyridoxamine 5'-phosphate shows no substrate inhibition
-
pyridoxal 5'-phosphate
-
product inhibition is of a mixed-type nature and results from binding of this vitamer at an allosteric site
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.368
pyridoxal 5'-phosphate
-
recombinant enzyme after cleavage from fusion protein
additional information
additional information
-
KM-values of mutant enzymes H199A, H199N, R197E, R197M, Y17F, R14E, R14M
-
0.0024
pyridoxine 5'-phosphate
pH 7.6, 37°C, mutant enzyme K145A/F177A
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
0.4
pyridoxamine 5'-phosphate
-
recombinant enzyme after cleavage from fusion protein
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
33
pyridoxal 5'-phosphate
-
recombinant enzyme after cleavage from fusion protein
additional information
additional information
-
turnover numbers of mutant enzymes H199A, H199N, R197E, R197M, Y17F, R14E, R14M
-
0.05
pyridoxine 5'-phosphate
pH 7.6, 37°C, mutant enzyme N84W/K145A/F177A
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/R24L/R215L
28
pyridoxamine 5'-phosphate
-
recombinant enzyme after cleavage from fusion protein
0.2
pyridoxine 5'-phosphate
-
recombinant enzyme, in phosphate and HEPES buffer at pH 7.6
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.008
pyridoxal 5'-phosphate
-
pH and temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.5 - 10
-
pyridoxamine phosphate oxidase activity remains nearly constant between pH 8.5 and 10.0
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5 - 10
-
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
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
-
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
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
51000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
-
1 * 25500, recombinant enzyme after cleavage from fusion protein, gel filtration
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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/R24L/R21L
complete loss of allosteric properties. The Tm-value is about 2°C lower than the Tm-value of the wild-type enzyme
K72A
-
the mutant shows a sharp decrease of the catalytic activity compared to the wild type enzyme
K72P
-
the mutant shows a sharp decrease of the catalytic activity compared to the wild type enzyme
K72Q
-
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
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
70
65
-
no loss in activity after incubation at temperatures below 50°C, 30% to 40% activity loss after 15 min at 65°C
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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.
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
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
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
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
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
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
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
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
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
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)
EXTERNAL LINKS (specific for EC-Number 1.4.3.5)
Transporter Classification Database (TCDB): 2.A.7.2.4
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
