Information on EC 1.4.3.5 - pyridoxal 5'-phosphate synthase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Mark a special word or phrase in this record:
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


The expected taxonomic range for this enzyme is: Bacteria, Eukaryota

EC NUMBER
COMMENTARY
1.4.3.5
-
RECOMMENDED NAME
GeneOntology No.
pyridoxal 5'-phosphate synthase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
pyridoxamine 5'-phosphate + H2O + O2 = pyridoxal 5'-phosphate + NH3 + H2O2
show the reaction diagram
enzyme is not stereospecific and catalyzes removal of either pro-R or pro-S hydrogen from 4-methylene of pyridoxamine 5' phosphate
-
pyridoxamine 5'-phosphate + H2O + O2 = pyridoxal 5'-phosphate + NH3 + H2O2
show the reaction diagram
kinetic mechanims via either a binary or a ternary complex mechanism, depending on nature of substrate, ternary complex mechanism with pyridoxamine 5'-phosphate
-
pyridoxamine 5'-phosphate + H2O + O2 = pyridoxal 5'-phosphate + NH3 + H2O2
show the reaction diagram
reaction mechanism
-
pyridoxamine 5'-phosphate + H2O + O2 = pyridoxal 5'-phosphate + NH3 + H2O2
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
-
-
-
-
pyridoxine 5'-phosphate + O2 = pyridoxal 5'-phosphate + H2O2
show the reaction diagram
reaction mechanism
-
pyridoxine 5'-phosphate + O2 = pyridoxal 5'-phosphate + H2O2
show the reaction diagram
-
-
-
-
pyridoxine 5'-phosphate + O2 = pyridoxal 5'-phosphate + H2O2
show the reaction diagram
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 ACCESSION NO.
COMMENTARY
LITERATURE
Deamination
-
-
-
-
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
4-amino-2-methyl-5-phosphomethylpyrimidine biosynthesis (yeast)
-
Metabolic pathways
-
pyridoxal 5'-phosphate biosynthesis I
-
pyridoxal 5'-phosphate salvage I
-
pyridoxal 5'-phosphate salvage II (plants)
-
Vitamin B6 metabolism
-
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.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
FprA protein
-
-
-
-
oxidase, pyridoxamine phosphate
-
-
-
-
PMP oxidase
-
-
-
-
PMP oxidase
-
-
PNP oxidase
-
-
PNP/PMP oxidase
-
-
-
-
PNP/PMP oxidase
-
-
PNPO
Q1PCB0
-
PNPO
-
-
PNPO
-
-
PNPOx
-
-
-
-
PNPOx
-
-
PNPOx
Mycobacterium tuberculosis Rv2074
-
-
-
pyridox(am)ine 5'-phosphate oxidase
-
-
pyridoxal 5'-phosphate synthase
-
-
pyridoxal 5'-phosphate synthetic enzyme
-
-
pyridoxamine (pyridoxine) 5'-phosphate oxidase
-
-
pyridoxamine (pyridoxine) 5'-phosphate oxidase
-
-
pyridoxamine (pyridoxine) 5'-phosphate oxidase
-
-
pyridoxamine (pyridoxine) 5'-phosphate oxidase
-
-
pyridoxamine (pyridoxine) 5'-phosphate oxidase activity
-
-
pyridoxamine (pyridoxine) 5-phosphate:O2 oxidoreductase (deaminating)
-
-
pyridoxamine (pyridoxine) 5-phosphate:O2 oxidoreductase (deaminating)
-
-
pyridoxamine 5'-phosphate oxidase
-
-
-
-
pyridoxamine 5'-phosphate oxidase
-
-
pyridoxamine phosphate oxidase
-
-
-
-
pyridoxamine phosphate oxidase
-
-
pyridoxamine-5-phosphate oxidase
-
-
pyridoxamine-phosphate oxidase
-
-
-
-
pyridoxaminephosphate oxidase (EC 1.4.3.5: deaminating)
-
-
-
-
pyridoxine (pyridoxamine) 5 '-phosphate oxidase
-
-
pyridoxine (pyridoxamine) 5'-phosphate oxidase
-
-
-
-
pyridoxine (pyridoxamine) 5'-phosphate oxidase
-
-
pyridoxine (pyridoxamine) 5'-phosphate oxidase
-
-
pyridoxine (pyridoxamine) phosphate oxidase
-
-
-
-
pyridoxine (pyridoxamine) phosphate oxidase
-
-
pyridoxine 5'-phosphate oxidase
Q1PCB0
-
pyridoxine 5'-phosphate oxidase
-
-
pyridoxine 5'-phosphate oxidase
-
-
pyridoxine 5'-phosphate oxidase
Mycobacterium tuberculosis Rv2074
-
-
-
pyridoxine 5-phosphate oxidase
-
-
pyridoxine phosphate oxidase
-
-
pyridoxine-5'-phosphate oxidase
-
-
pyridoxine/pyridoxamine phosphate oxidase
-
-
CAS REGISTRY NUMBER
COMMENTARY
9029-21-4
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
gene AT5g49970
-
-
Manually annotated by BRENDA team
single copy PNPO gene
UniProt
Manually annotated by BRENDA team
Chloridazon-degrading bacterium
-
-
-
Manually annotated by BRENDA team
Flavobacterium sp. CB6
CB6
-
-
Manually annotated by BRENDA team
overview
-
-
Manually annotated by BRENDA team
gene PNPO
-
-
Manually annotated by BRENDA team
strains H37Rv and Rv1155
Uniprot
Manually annotated by BRENDA team
Mycobacterium tuberculosis Rv2074
strain Rv2074
-
-
Manually annotated by BRENDA team
no activity in Arthrobacter globiformis
-
-
-
Manually annotated by BRENDA team
no activity in Arthrobacter sp.
SuC 3
-
-
Manually annotated by BRENDA team
no activity in Arthrobacter sp. SuC 3
SuC 3
-
-
Manually annotated by BRENDA team
no activity in Bacillus cereus
-
-
-
Manually annotated by BRENDA team
no activity in Bacillus circulans
-
-
-
Manually annotated by BRENDA team
no activity in Bacillus pasteurii
-
-
-
Manually annotated by BRENDA team
no activity in Bacillus polymyxa
-
-
-
Manually annotated by BRENDA team
no activity in Bacillus subtilis
-
-
-
Manually annotated by BRENDA team
no activity in Micrococcus luteus
-
-
-
Manually annotated by BRENDA team
no activity in Nocardia sp.
CBS 2
-
-
Manually annotated by BRENDA team
no activity in Nocardia sp. CBS 2
CBS 2
-
-
Manually annotated by BRENDA team
Pseudomonas sp. CBS 4
CBS 4
-
-
Manually annotated by BRENDA team
Japanese radish
-
-
Manually annotated by BRENDA team
male sprague-dawley rats
-
-
Manually annotated by BRENDA team
no activity in Morris hepatoma 7777 cells
-
-
Manually annotated by BRENDA team
; 2 forms: FI and FII
-
-
Manually annotated by BRENDA team
strains FL100 and AL114
-
-
Manually annotated by BRENDA team
; wheat, properties of the enzyme induced by light may differ from those of a constitutive enzyme
-
-
Manually annotated by BRENDA team
isozymes: E1 and E2; two isozymes E-I and E-II
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
physiological function
-
a glutamine amidotransferase consisting of the synthase Pdx1 and its glutaminase partner, Pdx2, form a complex that directly synthesizes pyridoxal from ribose 5-phosphate, glyceraldehyde 3-phosphate, and glutamine. The protein complex displays an ornate architecture consisting of 24 subunits, two hexameric rings of 12 Pdx1 subunits to which 12 Pdx2 subunits attach, with the glutaminase and synthase active sites remote from each other; fluorescence spectrophotometry is used to demonstrate that the Pdx1 C-terminus is indispensable for pyridoxal synthase activity and mediates intersubunit cross-talk within the enzyme complex. The C-terminus can act as a flexible lid, bridging as well as shielding the active site of an adjacent protomer in Pdx1. Ribose 5-phosphate binding triggers strong cooperativity in Pdx1, and the affinity for this substrate is substantially enhanced upon interaction with the Michaelis complex of Pdx2 and glutamine
physiological function
-
upregulation of PNPO expression may be involved in dendritic spine reorganization, which in turn, promotes the reverberation of recurrent excitatory networks in the hippocampus following status epilepticus. Activity-dependent regulation of PLP synthetic enzyme levels may play a role in tissue excitability in the hippocampus via various pathways
physiological function
-
the enzyme plays a role in resistance to photooxidative damage as well as root development
malfunction
-
an RNAi mutant shows sensitivity to high light
additional information
-
neurological diseases lead to upregulation of PNPO, immunoreactivities are mainly increased in glutamatergic principal neurons, dentate granule cells and CA1 pyramidal cells, and astrocytes independently of 4-aminobutyric acid levels, overview
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
5'-homopyridoxine-phosphate + H2O + O2
homopyridoxal 5'-phosphate + H2O2
show the reaction diagram
-
-
-
?
5'-phospho-pyridoxal-O-carboxymethyloxime + H2O + O2
O-carboxymethylpyridoxal 5'-phosphate + hydroxylamine + H2O2
show the reaction diagram
-
-
-
?
5'-phospho-pyridoxaloxime + H2O + O2
pyridoxal 5'-phosphate + hydroxylamine + H2O2
show the reaction diagram
-
-
-
?
5'-phospho-pyridoxyl-2-aminobutyrate + H2O + O2
pyridoxal 5'-phosphate + 2-aminobutyrate + H2O2
show the reaction diagram
-
110% of activity with pyridoxamine 5'-phosphate
-
?
5'-phospho-pyridoxyl-3-alanine + H2O + O2
pyridoxal 5'-phosphate + alanine + H2O2
show the reaction diagram
-
-
-
?
5'-phospho-pyridoxyl-3-alanine + H2O + O2
pyridoxal 5'-phosphate + alanine + H2O2
show the reaction diagram
-
85% of activity with pyridoxamine 5'-phosphate
-
?
5'-phospho-pyridoxyl-3-aminobenzoate + H2O + O2
pyridoxal 5'-phosphate + 3-aminobenzoate + H2O2
show the reaction diagram
-
-
-
?
5'-phospho-pyridoxyl-4-aminobenzoate + H2O + O2
pyridoxal 5'-phosphate + 4-aminobenzoate + H2O2
show the reaction diagram
-
-
-
?
5'-phospho-pyridoxyl-4-aminobutyrate + H2O + O2
pyridoxal 5'-phosphate + 4-aminobutyrate + H2O2
show the reaction diagram
-
-
-
?
5'-phospho-pyridoxyl-4-aminonitrobenzene + H2O + O2
pyridoxal 5'-phosphate + 4-aminonitrobenzene + H2O2
show the reaction diagram
-
-
-
?
5'-phospho-pyridoxyl-4-aminophenol + H2O + O2
pyridoxal 5'-phosphate + 4-aminophenol + H2O2
show the reaction diagram
-
-
-
?
5'-phospho-pyridoxyl-5-aminovalerate + H2O + O2
pyridoxal 5'-phosphate + 5-aminovalerate + H2O2
show the reaction diagram
-
-
-
?
5'-phospho-pyridoxyl-5-aminovalerate + H2O + O2
pyridoxal 5'-phosphate + 5-aminovalerate + H2O2
show the reaction diagram
-
-
-
-
-
5'-phospho-pyridoxyl-aniline + H2O + O2
pyridoxal 5'-phosphate + aniline + H2O2
show the reaction diagram
-
-
-
?
5'-phospho-pyridoxyl-benzylamine + H2O + O2
pyridoxal 5'-phosphate + benzylamine + H2O2
show the reaction diagram
-
120% of activity with pyridoxamine 5'-phosphate
-
?
5'-phospho-pyridoxyl-D-2-aminobutyrate + H2O + O2
pyridoxal 5'-phosphate + D-2-aminobutyrate + H2O2
show the reaction diagram
-
120% of activity with pyridoxamine 5'-phosphate
-
?
5'-phospho-pyridoxyl-D-alanine + H2O + O2
pyridoxal 5'-phosphate + D-alanine + H2O2
show the reaction diagram
-
130% of activity with pyridoxamine 5'-phosphate
-
?
5'-phospho-pyridoxyl-D-leucine + H2O + O2
pyridoxal 5'-phosphate + D-leucine + H2O2
show the reaction diagram
-
120% of activity with pyridoxamine 5'-phosphate
-
?
5'-phospho-pyridoxyl-D-tyrosine + H2O + O2
pyridoxal 5'-phosphate + D-tyrosine + H2O2
show the reaction diagram
-
55% of activity with pyridoxamine 5'-phosphate
-
?
5'-phospho-pyridoxyl-glycine + H2O + O2
pyridoxal 5'-phosphate + glycine + H2O2
show the reaction diagram
-
-
-
-
-
5'-phospho-pyridoxyl-glycine + H2O + O2
pyridoxal 5'-phosphate + glycine + H2O2
show the reaction diagram
-
110% of activity with pyridoxamine 5'-phosphate
-
?
5'-phospho-pyridoxyl-L-2-aminobutyrate + H2O + O2
pyridoxal 5'-phosphate + L-2-aminobutyrate + H2O2
show the reaction diagram
-
-
-
?
5'-phospho-pyridoxyl-L-alanine + H2O + O2
pyridoxal 5'-phosphate + L-alanine + H2O2
show the reaction diagram
-
140% of activity with pyridoxamine 5'-phosphate
-
?
5'-phospho-pyridoxyl-L-leucine + H2O + O2
pyridoxal 5'-phosphate + L-leucine + H2O2
show the reaction diagram
-
86% of activity with pyridoxamine 5'-phosphate
-
?
5'-phospho-pyridoxyl-L-phenylalanine + H2O + O2
pyridoxal 5'-phosphate + L-phenylalanine + H2O2
show the reaction diagram
-
54% of activity with pyridoxamine 5'-phosphate
-
?
5'-phospho-pyridoxyl-L-serine + H2O + O2
pyridoxal 5'-phosphate + L-serine + H2O2
show the reaction diagram
-
39% of activity with pyridoxamine 5'-phosphate
-
?
5'-phospho-pyridoxyl-L-tryptophan + H2O + O2
pyridoxal 5'-phosphate + L-tryptophan + H2O2
show the reaction diagram
-
18% of activity with pyridoxamine 5'-phosphate
-
?
5'-phospho-pyridoxyl-L-tyrosine + H2O + O2
pyridoxal 5'-phosphate + L-tyrosine + H2O2
show the reaction diagram
-
57% of activity with pyridoxamine 5'-phosphate
-
?
alpha-N-(5'-phospho-4'-pyridoxyl)-ornithine + O2 + H2O
pyridoxal 5'-phosphate + alpha-ornithine + H2O2
show the reaction diagram
-
-
-
?
N-(5'-phospho-4'-pyridoxyl)-N'-(1-naphthyl)ethylenediamine + H2O + O2
pyridoxal 5'-phosphate + N-(1-naphthyl)-ethylenediamine + H2O2
show the reaction diagram
-
-
-
?
N-(5'-phospho-4'-pyridoxyl)-N'-(1-naphthyl-5-sulfonate)-ethylenediamine + H2O + O2
pyridoxal 5'-phosphate + N-(1-naphthyl-5-sulfonate)-ethylenediamine + H2O2
show the reaction diagram
-
-
-
?
N-(5'-phospho-4'-pyridoxyl)-N'-(9-acridyl)ethylenediamine + H2O + O2
pyridoxal 5'-phosphate + N-(9-acridyl)ethylenediamine + H2O2
show the reaction diagram
-
-
-
?
N-(5'-phospho-4'-pyridoxyl)-N'-(dansyl)ethylenediamine + H2O + O2
pyridoxal 5'-phosphate + N-(dansyl)ethylenediamine + H2O2
show the reaction diagram
-
-
-
?
N-(5'-phospho-4'-pyridoxyl)-N'-(dansyl)pentylenediamine + H2O + O2
pyridoxal 5'-phosphate + N-(dansyl)pentylenediamine + H2O2
show the reaction diagram
-
-
-
?
N-(5'-phosphopyridoxyl)-tryptamine + FMN + H2O
?
show the reaction diagram
-
radio-labeled substrate N-(5'-phosphopyridoxyl)-[3H]tryptamine
-
-
?
N-phosphopyridoxyl tryptamine + H2O + O2
pyridoxal 5'-phosphate + tryptamine + H2O2
show the reaction diagram
-
-
-
?
N10-(5'-phosphopyridoxyl)-1,10-diaminodecane + H2O + O2
pyridoxal 5'-phosphate + 1,10-diaminodecane + H2O2
show the reaction diagram
-
-
-
-
-
N10-(5'-phosphopyridoxyl)-1,10-diaminodecane + H2O + O2
pyridoxal 5'-phosphate + 1,10-diaminodecane + H2O2
show the reaction diagram
-
-
-
?
N2-acetyl-N6-(5'-phosphopyridoxyl)-L-lysine + H2O + O2
pyridoxal 5'-phosphate + N2-acetyl-L-lysine + H2O2
show the reaction diagram
-
-
-
?
pyridoxamine 5'-phosphate + FMN + H2O + 2 H+
pyridoxal 5'-phosphate + FMNH2 + NH3
show the reaction diagram
-
-
-
-
?
pyridoxamine 5'-phosphate + FMN + H2O + 2 H+
pyridoxal 5'-phosphate + FMNH2 + NH3
show the reaction diagram
-
-
-
-
?
pyridoxamine 5'-phosphate + FMN + H2O + 2 H+
pyridoxal 5'-phosphate + FMNH2 + NH3
show the reaction diagram
-
-
-
-
?
pyridoxamine 5'-phosphate + FMN + H2O + 2 H+
pyridoxal 5'-phosphate + FMNH2 + NH3
show the reaction diagram
-
-
-
-
?
pyridoxamine 5'-phosphate + FMN + H2O + 2 H+
pyridoxal 5'-phosphate + FMNH2 + NH3
show the reaction diagram
-
-
-
-
?
pyridoxamine 5'-phosphate + FMN + H2O + 2 H+
pyridoxal 5'-phosphate + FMNH2 + NH3
show the reaction diagram
-
-
-
-
?
pyridoxamine 5'-phosphate + FMN + H2O + 2 H+
pyridoxal 5'-phosphate + FMNH2 + NH3
show the reaction diagram
-
-
-
-
?
pyridoxamine 5'-phosphate + FMN + H2O + 2 H+
pyridoxal 5'-phosphate + FMNH2 + NH3
show the reaction diagram
-
1.6fold preferred substrate of isozyme E-II
-
-
?
pyridoxamine 5'-phosphate + FMN + H2O + 2 H+
pyridoxal 5'-phosphate + FMNH2 + NH3
show the reaction diagram
-
preferred substrate of the PMP oxidase isozyme
-
-
?
pyridoxamine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + NH3 + H2O2
show the reaction diagram
-
-
-
?
pyridoxamine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + NH3 + H2O2
show the reaction diagram
-
-
-
?
pyridoxamine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + NH3 + H2O2
show the reaction diagram
-
-
-
?
pyridoxamine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + NH3 + H2O2
show the reaction diagram
-
-
-
?
pyridoxamine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + NH3 + H2O2
show the reaction diagram
-
-
-
?
pyridoxamine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + NH3 + H2O2
show the reaction diagram
-
-
-
?
pyridoxamine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + NH3 + H2O2
show the reaction diagram
P0AFI7
-
-
?
pyridoxamine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + NH3 + H2O2
show the reaction diagram
-
-
-
-
?
pyridoxamine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + NH3 + H2O2
show the reaction diagram
-
-
-
?
pyridoxamine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + NH3 + H2O2
show the reaction diagram
-
-
-
?
pyridoxamine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + NH3 + H2O2
show the reaction diagram
-
-
-
-
?
pyridoxamine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + NH3 + H2O2
show the reaction diagram
-
-
-
?
pyridoxamine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + NH3 + H2O2
show the reaction diagram
-
-
-
?
pyridoxamine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + NH3 + H2O2
show the reaction diagram
-
-
-
?
pyridoxamine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + NH3 + H2O2
show the reaction diagram
-
-
-
?
pyridoxamine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + NH3 + H2O2
show the reaction diagram
-
-
-
?
pyridoxamine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + NH3 + H2O2
show the reaction diagram
-
-
-
?
pyridoxamine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + NH3 + H2O2
show the reaction diagram
-
-
-
?
pyridoxamine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + NH3 + H2O2
show the reaction diagram
-
-
-
?
pyridoxamine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + NH3 + H2O2
show the reaction diagram
-
-
-
?
pyridoxamine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + NH3 + H2O2
show the reaction diagram
-
-
-
?
pyridoxamine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + NH3 + H2O2
show the reaction diagram
-
-
-
?
pyridoxamine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + NH3 + H2O2
show the reaction diagram
-
-
-
?
pyridoxamine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + NH3 + H2O2
show the reaction diagram
-
-
-
?
pyridoxamine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + NH3 + H2O2
show the reaction diagram
-
-
-
?
pyridoxamine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + NH3 + H2O2
show the reaction diagram
-
-
-
?
pyridoxamine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + NH3 + H2O2
show the reaction diagram
-
-
-
?
pyridoxamine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + NH3 + H2O2
show the reaction diagram
-
-
-
?
pyridoxamine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + NH3 + H2O2
show the reaction diagram
-
-
-
?
pyridoxamine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + NH3 + H2O2
show the reaction diagram
-
-
-
?
pyridoxamine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + NH3 + H2O2
show the reaction diagram
-
-
-
?
pyridoxamine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + NH3 + H2O2
show the reaction diagram
-
-
-
?
pyridoxamine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + NH3 + H2O2
show the reaction diagram
-
-
-
?
pyridoxamine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + NH3 + H2O2
show the reaction diagram
-
-
-
?
pyridoxamine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + NH3 + H2O2
show the reaction diagram
-
-
-
?
pyridoxamine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + NH3 + H2O2
show the reaction diagram
-
-
-
?
pyridoxamine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + NH3 + H2O2
show the reaction diagram
-
-
-
?
pyridoxamine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + NH3 + H2O2
show the reaction diagram
-
-
-
?
pyridoxamine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + NH3 + H2O2
show the reaction diagram
-
-
-
?
pyridoxamine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + NH3 + H2O2
show the reaction diagram
-
-
-
?
pyridoxamine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + NH3 + H2O2
show the reaction diagram
-
-
-
?
pyridoxamine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + NH3 + H2O2
show the reaction diagram
-
-
-
?
pyridoxamine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + NH3 + H2O2
show the reaction diagram
-
-
-
?
pyridoxamine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + NH3 + H2O2
show the reaction diagram
-
-
-
-
?
pyridoxamine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + NH3 + H2O2
show the reaction diagram
-
-
-
?
pyridoxamine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + NH3 + H2O2
show the reaction diagram
-
-
-
?
pyridoxamine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + NH3 + H2O2
show the reaction diagram
-
-
-
?
pyridoxamine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + NH3 + H2O2
show the reaction diagram
-
-
-
?
pyridoxamine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + NH3 + H2O2
show the reaction diagram
-
-
-
?
pyridoxamine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + NH3 + H2O2
show the reaction diagram
-
-
-
?
pyridoxamine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + NH3 + H2O2
show the reaction diagram
-
-
-
?
pyridoxamine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + NH3 + H2O2
show the reaction diagram
-
-
-
?
pyridoxamine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + NH3 + H2O2
show the reaction diagram
-
-
-
?
pyridoxamine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + NH3 + H2O2
show the reaction diagram
-
-
-
?
pyridoxamine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + NH3 + H2O2
show the reaction diagram
-
-
-
?
pyridoxamine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + NH3 + H2O2
show the reaction diagram
Chloridazon-degrading bacterium
-
-
-
?
pyridoxamine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + NH3 + H2O2
show the reaction diagram
-, Q1PCB0
-
-
-
?
pyridoxamine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + NH3 + H2O2
show the reaction diagram
-
no oxidation of the unphosphorylated analogs of pyridoxamine phosphate, pyridoxine phosphate and N-(phosphopyridoxyl)amines
-
?
pyridoxamine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + NH3 + H2O2
show the reaction diagram
-
E II uses pyridoxine 5'-phosphate and pyridoxamine 5'-phosphate, isozymes E I uses only pyridoxine 5'-phosphate as substrate
-
?
pyridoxamine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + NH3 + H2O2
show the reaction diagram
-
6 to 7fold more active as with pyridoxamine 5'-phosphate
-
?
pyridoxamine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + NH3 + H2O2
show the reaction diagram
-
enzyme is not stereospecific, catalyzes equally well removal of either pro-R or pro-S-hydrogen from the 4-methylene of pyridoxamine 5'-phosphate
-
?
pyridoxamine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + NH3 + H2O2
show the reaction diagram
-
in conjugation with pyridoxal kinase the enzyme is responsible for the formation of the coenzyme pyridoxal 5'-phosphate, from the B6 vitamers pyridoxine and pyridoxamine
-
?
pyridoxamine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + NH3 + H2O2
show the reaction diagram
-
may be the regulatory enzyme in the final step of pyridoxal 5'-phosphate biosynthesis
-
?
pyridoxamine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + NH3 + H2O2
show the reaction diagram
-
enzyme plays a role in regulation of vitamin B-6 metabolism in erythrocytes
-
?
pyridoxamine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + NH3 + H2O2
show the reaction diagram
-
terminal step in de novo biosynthesis of pyridoxal 5'-phosphate
-
-
?
pyridoxamine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + NH3 + H2O2
show the reaction diagram
-
terminal step in de novo biosynthesis of pyridoxal 5'-phosphate
-
-
?
pyridoxamine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + NH3 + H2O2
show the reaction diagram
-
the enzyme prefers pyridoxine 5'-phosphate over pyridoxamine 5'-phosphate
-
-
?
pyridoxamine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + NH3 + H2O2
show the reaction diagram
Pseudomonas sp. CBS 4, Flavobacterium sp. CB6
-
-
-
?
pyridoxine 5'-phosphate + FMN
pyridoxal 5'-phosphate + FMNH2
show the reaction diagram
-
-
-
-
?
pyridoxine 5'-phosphate + FMN
pyridoxal 5'-phosphate + FMNH2
show the reaction diagram
-
-
-
-
?
pyridoxine 5'-phosphate + FMN
pyridoxal 5'-phosphate + FMNH2
show the reaction diagram
-
-
-
-
-
pyridoxine 5'-phosphate + FMN
pyridoxal 5'-phosphate + FMNH2
show the reaction diagram
-
-
-
-
?
pyridoxine 5'-phosphate + FMN
pyridoxal 5'-phosphate + FMNH2
show the reaction diagram
-
-
-
-
?
pyridoxine 5'-phosphate + FMN
pyridoxal 5'-phosphate + FMNH2
show the reaction diagram
-
-
-
-
?
pyridoxine 5'-phosphate + FMN
pyridoxal 5'-phosphate + FMNH2
show the reaction diagram
-
-
-
-
?
pyridoxine 5'-phosphate + FMN
pyridoxal 5'-phosphate + FMNH2
show the reaction diagram
-
-
-
-
?
pyridoxine 5'-phosphate + FMN
pyridoxal 5'-phosphate + FMNH2
show the reaction diagram
-
9fold preferred substrate of isozyme E-I
-
-
?
pyridoxine 5'-phosphate + FMN
pyridoxal 5'-phosphate + FMNH2
show the reaction diagram
-
preferred substrate of the PNP oxidase isozyme
-
-
?
pyridoxine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + H2O2
show the reaction diagram
-
-
-
?
pyridoxine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + H2O2
show the reaction diagram
-
-
-
-
?
pyridoxine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + H2O2
show the reaction diagram
-
-
-
?
pyridoxine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + H2O2
show the reaction diagram
-
-
-
?
pyridoxine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + H2O2
show the reaction diagram
-
-
-
?
pyridoxine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + H2O2
show the reaction diagram
-
-
-
?
pyridoxine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + H2O2
show the reaction diagram
-
-
-
?
pyridoxine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + H2O2
show the reaction diagram
-
-
-
?
pyridoxine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + H2O2
show the reaction diagram
-
-
-
-
?
pyridoxine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + H2O2
show the reaction diagram
-
-
-
-
?
pyridoxine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + H2O2
show the reaction diagram
-, Q1PCB0
-
-
-
?
pyridoxine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + H2O2
show the reaction diagram
-
preferred substrate
-
-
?
pyridoxine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + H2O2
show the reaction diagram
-
terminal step in de novo biosynthesis of pyridoxal 5'-phosphate
-
-
?
pyridoxine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + H2O2
show the reaction diagram
-
terminal step in de novo biosynthesis of pyridoxal 5'-phosphate
-
-
?
pyridoxine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + H2O2
show the reaction diagram
-
the enzyme prefers pyridoxine 5'-phosphate over pyridoxamine 5'-phosphate
-
-
?
pyridoxine 5'-phosphate + O2
pyridoxal 5'-phosphate + H2O2
show the reaction diagram
-
-
-
-
?
epsilon-pyridoxyllysine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + lysine + H2O2
show the reaction diagram
-
-
-
?
additional information
?
-
-
mutations in the PNPO gene encoding pyridox(am)ine 5'-phosphate oxidase cause neonatal epileptic encephalopathy
-
-
-
additional information
?
-
-
a 5'-phosphate moiety is absolutely required for activity, substrate specificities with various N-(phosphopyridoxyl)amines, overview, no activity with pyridoxamine, N-(pyridoxyl)-glycine, N-(pyridoxyl)-S-alanine, or N-(pyridoxyl)-L-tyrosine
-
-
-
additional information
?
-
-
substrate synthesis and preparation, fluorescence labeling with N-(1-naphthyl-5-sulfonate)-ethylenediamine, and N-(9-acridyl)-ethylenediamine, overview
-
-
-
additional information
?
-
-
the yeast contains PMP oxidase and PNP oxidase isozymes, which can be separated by calcium phosphate gel chromatography
-
-
-
additional information
?
-
-
at the Pdx1 active site, a pentose phosphate and triose phosphate sugar (i.e. ribose 5-phosphate and glyceraldehyde 3-phosphate) are combined along with ammonia to form pyridoxal
-
-
-
additional information
?
-
-
the enzyme does not recognize pyridoxamine 5'-phosphate as substrate
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
pyridoxamine 5'-phosphate + FMN + H2O + 2 H+
pyridoxal 5'-phosphate + FMNH2 + NH3
show the reaction diagram
-
-
-
-
?
pyridoxamine 5'-phosphate + FMN + H2O + 2 H+
pyridoxal 5'-phosphate + FMNH2 + NH3
show the reaction diagram
-
-
-
-
?
pyridoxamine 5'-phosphate + FMN + H2O + 2 H+
pyridoxal 5'-phosphate + FMNH2 + NH3
show the reaction diagram
-
-
-
-
?
pyridoxamine 5'-phosphate + FMN + H2O + 2 H+
pyridoxal 5'-phosphate + FMNH2 + NH3
show the reaction diagram
-
-
-
-
?
pyridoxamine 5'-phosphate + FMN + H2O + 2 H+
pyridoxal 5'-phosphate + FMNH2 + NH3
show the reaction diagram
-
-
-
-
?
pyridoxamine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + NH3 + H2O2
show the reaction diagram
-
-
-
-
?
pyridoxamine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + NH3 + H2O2
show the reaction diagram
-
-
-
-
?
pyridoxamine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + NH3 + H2O2
show the reaction diagram
-
-
-
-
?
pyridoxamine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + NH3 + H2O2
show the reaction diagram
-, Q1PCB0
-
-
-
?
pyridoxamine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + NH3 + H2O2
show the reaction diagram
-
in conjugation with pyridoxal kinase the enzyme is responsible for the formation of the coenzyme pyridoxal 5'-phosphate, from the B6 vitamers pyridoxine and pyridoxamine
-
?
pyridoxamine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + NH3 + H2O2
show the reaction diagram
-
may be the regulatory enzyme in the final step of pyridoxal 5'-phosphate biosynthesis
-
?
pyridoxamine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + NH3 + H2O2
show the reaction diagram
-
enzyme plays a role in regulation of vitamin B-6 metabolism in erythrocytes
-
?
pyridoxamine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + NH3 + H2O2
show the reaction diagram
-
terminal step in de novo biosynthesis of pyridoxal 5'-phosphate
-
-
?
pyridoxamine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + NH3 + H2O2
show the reaction diagram
-
terminal step in de novo biosynthesis of pyridoxal 5'-phosphate
-
-
?
pyridoxine 5'-phosphate + FMN
pyridoxal 5'-phosphate + FMNH2
show the reaction diagram
-
-
-
-
?
pyridoxine 5'-phosphate + FMN
pyridoxal 5'-phosphate + FMNH2
show the reaction diagram
-
-
-
-
?
pyridoxine 5'-phosphate + FMN
pyridoxal 5'-phosphate + FMNH2
show the reaction diagram
-
-
-
-
?
pyridoxine 5'-phosphate + FMN
pyridoxal 5'-phosphate + FMNH2
show the reaction diagram
-
-
-
-
?
pyridoxine 5'-phosphate + FMN
pyridoxal 5'-phosphate + FMNH2
show the reaction diagram
-
-
-
-
?
pyridoxine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + H2O2
show the reaction diagram
-
-
-
-
?
pyridoxine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + H2O2
show the reaction diagram
-
-
-
-
?
pyridoxine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + H2O2
show the reaction diagram
-
-
-
-
?
pyridoxine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + H2O2
show the reaction diagram
-, Q1PCB0
-
-
-
?
pyridoxine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + H2O2
show the reaction diagram
-
preferred substrate
-
-
?
pyridoxine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + H2O2
show the reaction diagram
-
terminal step in de novo biosynthesis of pyridoxal 5'-phosphate
-
-
?
pyridoxine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + H2O2
show the reaction diagram
-
terminal step in de novo biosynthesis of pyridoxal 5'-phosphate
-
-
?
pyridoxine 5'-phosphate + O2
pyridoxal 5'-phosphate + H2O2
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
mutations in the PNPO gene encoding pyridox(am)ine 5'-phosphate oxidase cause neonatal epileptic encephalopathy
-
-
-
additional information
?
-
-
the enzyme does not recognize pyridoxamine 5'-phosphate as substrate
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
FAD
-
about 0.1% as active as FMN
FAD
-
bound poorly to apoenzyme
FMN
-
binds 1 mol of FMN per mol of dimer; flavoprotein
FMN
-
bound, required
FMN
-
analogs modified at position 2, 3, 7, 8, 8alpha and at the ribityl side chain are all bound by the apoenzyme but less tightly than FMN; binds 1 mol of FMN per mol of dimer
FMN
-
1 mol of FMN per mol of enzyme
FMN
-
2 molecules of FMN bound per homodimer
FMN
-
two molecules of FMN are noncovalently bound to the dimeric form of oxidase
FMN
-
contains one FMN molecule per dimer
additional information
-
specific for flavin-phosphate
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
potassium nitrate
-
in culture medium, activates PNP oxidase activity 2fold in callus culture, no activation of PMP oxidase
ammonium
-
in culture medium, activates PMP oxidase activity in callus culture by about 30%, no activation of PNP oxidase
additional information
-
neutral salts, such as LiCl, KCl, NaCl, KBr, KI, and KSCN, both activate and denature the enzyme
additional information
-
no requirement for bivalent cations
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2,3-Butanedione
-
10 mM, complete inhibition after 50 min in borate buffer, inhibition is fully reversible upon removal of borate
2,4-pentandione
-
0.3 mM, approx. 90% inhibition of holoenzyme
4-chloromercuribenzoate
-
0.1 mM, 90-95% inhibition
4-deoxypyridoxine 5'-phosphate
-
0.1 mM, 42% inhibition
4-deoxypyridoxine 5'-phosphate
-
-
4-deoxypyridoxine 5'-phosphate
-
competitive inhibition
4-Pyridoxic acid phosphate
-
0.1 mM, 33.5% inhibition
ammonium sulfate
-
1.9 M, E II: activation at short incubation time, E I: complete inactivation after 10 h incubation; inactivation of isozyme E-I after 10 h
Cd2+
-
0.5 mM, isozyme E I: insensitive, isozyme E II: 44% inhibition; 44% reduced activity of isozyme E-II, no inhibition of isozyme E-I
Cd2+
-
2.85 mM, 82% inhibition of pyridoxamine 5'-phosphate oxidation, 27% inhibition of pyridoxine oxidation
citrate-phosphate buffer
-
-
-
Cu2+
-
1 mM, 90-95% inhibition
Cu2+
-
2.85 mM, 38% inhibition of pyridoxamine 5'-phosphate oxidation, 23% inhibition of pyridoxine oxidation
diethyldicarbonate
-
1.2 mM, complete inactivation after 10 min, activity decrease of 60% can be restored by a 20 min incubation with 900 mM hydroxylamine, pyridoxal 5'-phosphate oxime protects from inactivation, inactivation is due to modification of histidine residues
Fe2+
-
2.85 mM, 44% inhibition of pyridoxamine 5'-phosphate oxidation, 81% inhibition of pyridoxine oxidation
-
Fe3+
-
2.85 mM, 26% inhibition of pyridoxamine 5'-phosphate oxidation, 50% inhibition of pyridoxine oxidation
-
guanidine hydrochloride urea
-
both activates and denatures the enzyme
Hg2+
-
1 mM, 90-95% inhibition
Hg2+
-
0.5 mM, isozyme E I: insensitive, isozyme E II: 54% inhibition; 72% reduced activity of isozyme E-II, no inhibition of isozyme E-I
Phenylglyoxal
-
pyridoxal 5'-phosphate protects
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
potent product inhibition
pyridoxal 5'-phosphate
-
competitive inhibition; competitive product inhibition, overview
pyridoxal 5'-phosphate
-
competitive inhibition
pyridoxal 5'-phosphate
-
competitive inhibition
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
competitive inhibitor
pyridoxal 5'-phosphate oxime
-
-
pyridoxaloxime 5'-phosphate
-
competitive inhibition
pyridoxaloxime 5'-phosphate
-
0.2 mM, 80% inhibition
pyridoxaloxime 5'-phosphate
-
-
pyridoxamine 5'-phosphate
-
substrate inhibition above 0.0006 mM
pyridoxine 5'-phosphate
-
substrate inhibition
pyridoxine 5'-phosphate
-
substrate inhibition
Urea
-
both activates and denatures the enzyme, reversible inactivation above 2.5 M, half-time of inactivation is 46 min at 2 M and 37C
Zn2+
-
0.5 mM, isozyme E I: insensitive, isozyme E II: 54% inhibition; 72% reduced activity of isozyme E-II, no inhibition of isozyme E-I
Zn2+
-
2.85 mM, 92% inhibition of pyridoxamine 5'-phosphate oxidation, 60% inhibition of pyridoxine oxidation
Hg2+
-
2.85 mM, 30% inhibition of pyridoxamine 5'-phosphate oxidation, 2% inhibition of pyridoxine oxidation
additional information
-
no inhibition by tryptophan metabolites
-
additional information
-
no substrate inhibition with pyridoxamine 5'-phosphate
-
additional information
-
pyridoxamine 5'-phosphate shows no substrate inhibition
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2-Aminobutanoate
-
activation
3-Hydroxyanthranilate
-
145% increase in pyridoxine 5-phosphate oxidase activity, 28% increase in pyridoxamine 5-phosphate oxidase activity
3-hydroxykynurenine
-
125% increase in pyridoxine 5-phosphate oxidase activity, 20% increase in pyridoxamine 5-phosphate oxidase activity
5-hydroxyindolacetate
-
125% increase in pyridoxine 5-phosphate oxidase activity, 9% increase in pyridoxamine 5-phosphate oxidase activity
5-hydroxytryptamine
-
20% increase in pyridoxamine 5-phosphate oxidase activity
alanine
-
activation
ammonium sulfate
-
short incubation activates isozyme E-II, not E-I
cysteine
-
activation
guanidine hydrochloride
-
500 mM, activation at low concentrations and brief periods of exposure, inactivation at higher concentrations and longer periods of exposure
tryptamine
-
27% increase in pyridoxamine 5-phosphate oxidase activity
Urea
-
2.0-2.5 M, rapid and reversible activation at low concentrations and brief periods of exposure, inactivation at higher concentrations and longer periods of exposure; both activates and denatures the enzyme, rapid and reversible activation at 2.0-2.5 M urea
valine
-
activation
xanthurenate
-
21% increase in pyridoxine 5-phosphate oxidase activity
guanidine hydrochloride urea
-
both activates and denatures the enzyme
additional information
-
the enzyme is induced by light without affecting the substrate specificity
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0059
-
5'-homopyridoxine-phosphate
-
-
0.0059
-
5'-methylpyridoxine-phosphate
-
-
0.031
-
5'-methylpyridoxine-phosphate
-
-
0.025
-
5'-phospho-pyridoxal-O-carboxymethyloxime
-
-
0.021
-
5'-phospho-pyridoxaloxime
-
-
0.01
-
5'-phospho-pyridoxyl-3-aminobenzoate
-
-
0.01
-
5'-phospho-pyridoxyl-4-aminobenzoate
-
-
0.03
-
5'-phospho-pyridoxyl-5-aminovalerate
-
-
0.01
-
5'-phospho-pyridoxyl-aniline
-
-
0.2
-
alpha-N-(5'-phospho-4'-pyridoxyl)-lysine
-
-
0.53
-
alpha-N-(5'-phospho-4'-pyridoxyl)-ornithine
-
-
0.11
-
N-(5'-phospho-4'-pyridoxyl)-beta-alanine
-
-
0.77
-
N-(5'-phospho-4'-pyridoxyl)-D-alanine
-
-
0.29
-
N-(5'-phospho-4'-pyridoxyl)-D-alpha-aminobutyrate
-
-
0.125
-
N-(5'-phospho-4'-pyridoxyl)-D-leucine
-
-
1.6
-
N-(5'-phospho-4'-pyridoxyl)-D-tyrosine
-
-
0.068
-
N-(5'-phospho-4'-pyridoxyl)-glycine
-
-
0.22
-
N-(5'-phospho-4'-pyridoxyl)-L-alanine
-
-
0.091
-
N-(5'-phospho-4'-pyridoxyl)-L-alpha-aminobutyrate
-
-
0.033
-
N-(5'-phospho-4'-pyridoxyl)-L-benzylamine
-
-
-
0.075
-
N-(5'-phospho-4'-pyridoxyl)-L-leucine
-
-
0.095
-
N-(5'-phospho-4'-pyridoxyl)-L-phenylalanine
-
-
0.13
-
N-(5'-phospho-4'-pyridoxyl)-L-serine
-
-
0.12
-
N-(5'-phospho-4'-pyridoxyl)-L-tryptophan
-
-
0.031
-
N-(5'-phospho-4'-pyridoxyl)-L-tyrosine
-
-
0.008
-
N-(5'-phospho-4'-pyridoxyl)-N'-(1-naphthyl)ethylenediamine
-
-
0.00065
-
N-Phosphopyridoxyl tryptamine
-
-
0.4
-
N10-(5'-phospho-4'-pyridoxyl)-1,10-diaminodecane
-
-
0.065
-
N2-acetyl-N6-(5'-phospho-pyridoxyl)-L-lysine
-
-
0.085
-
O2
-
cosubstrate pyridoxamine 5'-phosphate
0.182
-
O2
-
cosubstrate pyridoxine 5'-phosphate
0.035
-
Phospho-pyridoxyl-3-alanine
-
-
0.03
-
Phospho-pyridoxyl-4-aminobutyrate
-
-
0.03
-
Phospho-pyridoxyl-4-aminobutyrate
-
-
0.368
-
pyridoxal 5'-phosphate
-
recombinant enzyme after cleavage from fusion protein
0.021
-
pyridoxal phosphate oxime
-
-
0.025
-
pyridoxal phosphate-carboxymethyloxime ester
-
-
0.0013
-
pyridoxamine 5'-phosphate
-
pH 8.0
0.0013
-
pyridoxamine 5'-phosphate
-
measured in hemolysate
0.0021
-
pyridoxamine 5'-phosphate
-
pH 8.0, 25C, wild-type enzyme
0.0036
-
pyridoxamine 5'-phosphate
-
-
0.0062
-
pyridoxamine 5'-phosphate
-
pH 8.0, 25C, mutant enzyme DELTA1-56
0.0067
-
pyridoxamine 5'-phosphate
-
isozyme E-II, pH 8.0, 37C
0.008
-
pyridoxamine 5'-phosphate
-
enzyme activity in liver homogenate
0.01
-
pyridoxamine 5'-phosphate
-
-
0.01
-
pyridoxamine 5'-phosphate
-
immobilized enzyme
0.01
-
pyridoxamine 5'-phosphate
-
-
0.011
-
pyridoxamine 5'-phosphate
-
enzyme activity in liver homogenate
0.0112
-
pyridoxamine 5'-phosphate
-
; pH 8.0, 37C
0.013
-
pyridoxamine 5'-phosphate
-
-
0.015
-
pyridoxamine 5'-phosphate
-
enzyme activity in cytosol
0.018
-
pyridoxamine 5'-phosphate
-
soluble enzyme
0.018
-
pyridoxamine 5'-phosphate
-
pH 8.0, 37C
0.0187
-
pyridoxamine 5'-phosphate
-
in the presence of 1 M urea; pH 8.0, 37C, in presence of 1 M urea
0.024
-
pyridoxamine 5'-phosphate
-
pH 7.0, 37C; pure enzyme in 200 mM potassium phosphate pH 7.0
0.025
-
pyridoxamine 5'-phosphate
-
enzyme species FI which is assumed to be an artefact of the purification procedure
0.039
-
pyridoxamine 5'-phosphate
-
enzyme activity in liver homogenate in the presence of 0.005 mM pyridoxal 5'-phosphate
0.0417
-
pyridoxamine 5'-phosphate
-
in the presence of 2 M urea; pH 8.0, 37C, in presence of 2 M urea
0.105
-
pyridoxamine 5'-phosphate
-
recombinant enzyme
0.105
-
pyridoxamine 5'-phosphate
-
-
0.14
-
pyridoxamine 5'-phosphate
-
-
0.4
-
pyridoxamine 5'-phosphate
-
recombinant enzyme after cleavage from fusion protein
1
-
pyridoxamine 5'-phosphate
-
pH 7.6, 37C
0.1
-
pyridoxamine-5'-phosphate
-
-
0.0003
-
pyridoxine 5'-phosphate
-
; H199N mutant enzyme
0.00092
-
pyridoxine 5'-phosphate
-
-
0.001
-
pyridoxine 5'-phosphate
-
D49A and Y17F mutant enzyme
0.0012
-
pyridoxine 5'-phosphate
-
immobilized enzyme
0.002
-
pyridoxine 5'-phosphate
-
recombinant enzyme
0.002
-
pyridoxine 5'-phosphate
-
-
0.002
-
pyridoxine 5'-phosphate
-
R14E mutant enzyme
0.002
-
pyridoxine 5'-phosphate
-
pH 8.5, 37C
0.0026
-
pyridoxine 5'-phosphate
-
R14M mutant enzyme
0.0027
-
pyridoxine 5'-phosphate
-
soluble enzyme
0.0031
-
pyridoxine 5'-phosphate
-
-
0.004
-
pyridoxine 5'-phosphate
-
enzyme activity in liver homogenate
0.0062
-
pyridoxine 5'-phosphate
-
pH 8.0, 25C, wild-type enzyme
0.008
-
pyridoxine 5'-phosphate
-
isozyme E-II, pH 8.0, 37C
0.0082
-
pyridoxine 5'-phosphate
-
-
0.009
-
pyridoxine 5'-phosphate
-
enzyme species FI which is assumed to be an artefact of the purification procedure
0.013
-
pyridoxine 5'-phosphate
-
-
0.016
-
pyridoxine 5'-phosphate
-
pH 7.0, 37C; pure enzyme in 200 mM potassium phosphate pH 7.0
0.017
-
pyridoxine 5'-phosphate
-
enzyme activity in cytosol; enzyme activity in liver homogenate
0.02
-
pyridoxine 5'-phosphate
-
isozyme E-I, pH 8.0, 37C
0.02
-
pyridoxine 5'-phosphate
-
-
0.0208
-
pyridoxine 5'-phosphate
-
pH 8.0, 25C, mutant enzyme DELTA1-56
0.022
-
pyridoxine 5'-phosphate
-
enzyme activity in liver homogenate in the presence of 0.005 mM pyridoxal 5'-phosphate
0.0238
-
pyridoxine 5'-phosphate
-
; pH 8.0, 37C
0.025
-
pyridoxine 5'-phosphate
-
pH 8.0, 37C
0.03
-
pyridoxine 5'-phosphate
-
-
0.0667
-
pyridoxine 5'-phosphate
-
in the presence of 2 M urea; pH 8.0, 37C, in presence of 2 M urea
0.07
-
pyridoxine 5'-phosphate
-
H199A mutant enzyme
0.09
-
pyridoxine 5'-phosphate
-
R197M mutant enzyme
0.36
-
pyridoxine 5'-phosphate
-
in 25 mM potassium phosphate, pH 7.8 and 25C
1.8
-
pyridoxine 5'-phosphate
-
pH 7.6, 37C
2.4
-
pyridoxine 5'-phosphate
-
R197M mutant enzyme
additional information
-
additional information
-
steady-state kinetics
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
KM-values of mutant enzymes H199A, H199N, R197E, R197M, Y17F, R14E, R14M
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.04
-
5'-phospho-pyridoxyl-3-alanine
-
-
0.04
-
5'-phospho-pyridoxyl-4-aminobutyrate
-
-
0.035
-
5'-phospho-pyridoxyl-5-aminovalerate
-
-
0.01
-
5'-phospho-pyridoxyl-aniline
-
-
0.1
-
5'-phospho-pyridoxyl-m-aminobenzoate
-
-
0.1
-
5'-phospho-pyridoxyl-p-aminonitrobenzene
-
-
33
-
pyridoxal 5'-phosphate
-
recombinant enzyme after cleavage from fusion protein
0.009
-
pyridoxamine 5'-phosphate
-
-
0.103
-
pyridoxamine 5'-phosphate
-
-
0.103
-
pyridoxamine 5'-phosphate
-
-
0.2
-
pyridoxamine 5'-phosphate
-
pH 7.6, 37C
1.72
-
pyridoxamine 5'-phosphate
-
recombinant enzyme
28
-
pyridoxamine 5'-phosphate
-
recombinant enzyme after cleavage from fusion protein
0.008
-
pyridoxine 5'-phosphate
-
R197M mutant enzyme
0.01
-
pyridoxine 5'-phosphate
-
in 25 mM potassium phosphate, pH 7.8 and 25C
0.03
-
pyridoxine 5'-phosphate
-
H199N mutant enzyme; R197M mutant enzyme
0.06
-
pyridoxine 5'-phosphate
-
D49A mutant enzyme
0.09
-
pyridoxine 5'-phosphate
-
-
0.13
-
pyridoxine 5'-phosphate
-
-
0.13
-
pyridoxine 5'-phosphate
-
pH 8.5, 37C
0.14
-
pyridoxine 5'-phosphate
-
H199A mutant enzyme; R14M mutant enzyme
0.16
-
pyridoxine 5'-phosphate
-
R14E mutant enzyme
0.19
-
pyridoxine 5'-phosphate
-
pH 7.6, 37C
0.2
-
pyridoxine 5'-phosphate
-
recombinant enzyme, in phosphate and HEPES buffer at pH 7.6
0.3
-
pyridoxine 5'-phosphate
-
recombinant enzyme, in Tris buffer at pH 7.6
0.6
-
pyridoxine 5'-phosphate
-
Y17F mutant enzyme
0.7
-
pyridoxine 5'-phosphate
-
-
0.7
-
pyridoxine 5'-phosphate
-
-
0.76
-
pyridoxine 5'-phosphate
-
recombinant enzyme
0.004
-
5'-phospho-pyridoxyl-p-aminophenol
-
-
additional information
-
additional information
-
turnover numbers of mutant enzymes H199A, H199N, R197E, R197M, Y17F, R14E, R14M
-
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.028
-
pyridoxine 5'-phosphate
-
in 25 mM potassium phosphate, pH 7.8 and 25C
213120
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0018
-
4'-deoxypyridoxine-5'-phosphate
-
-
0.003
-
pyridoxal 5'-phosphate
-
pH 8.0, 37C; pure enzyme in 200 mM potassium phosphate pH 7.0 or enzyme activity in liver homogenate, substrate pyridoxamine 5' phosphate or pyridoxine 5'-phosphate
0.003
-
pyridoxal 5'-phosphate
-
-
0.0032
-
pyridoxal 5'-phosphate
-
pH 7.6, 37C
0.005
-
pyridoxal 5'-phosphate
-
pH and temperature not specified in the publication
0.008
-
pyridoxal 5'-phosphate
-
-
0.008
-
pyridoxal 5'-phosphate
-
pH and temperature not specified in the publication
0.019
-
pyridoxal 5'-phosphate
-
pH 8.0, 37C
0.025
-
pyridoxal 5'-phosphate
-
pH 8.0, 37C, in presence of 1 M urea
0.044
-
pyridoxal 5'-phosphate
-
pH 8.0, 37C, in presence of 2 M urea
3.8
-
pyridoxal 5'-phosphate
-
pH 8.5, 25C, pyridoxine 5'-phosphate as substrate, wild-type enzyme
23
-
pyridoxal 5'-phosphate
-
pH 8.5, 25C, pyridoxine 5'-phosphate as substrate, mutant enzyme DELTA1-56
0.002
-
pyridoxal 5'-phosphate oxime
-
-
0.05
-
pyridoxine 5'-phosphate
-
-
0.05
-
pyridoxine 5'-phosphate
-
substrate inhibition
0.105
-
4'-deoxypyridoxine-5'-phosphate
-
-
additional information
-
additional information
-
inhibition kinetics of urea, guanidinium hydrochloride, and neutral salts such as LiCl, KCl, NaCl, KBr, KI, and KSCN
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.2e-07
-
-
pyridoxine 5'-phosphate activity in seedlings
1e-06
-
-
pyridoxine 5'-phosphate activity in seedlings
1.2e-06
-
-
pyridoxine 5'-phosphate activity in root extracts
1.3e-06
-
-
pyridoxine 5'-phosphate activity in seedlings
1.5e-06
-
-
pyridoxine 5'-phosphate activity in seedlings
4.3e-06
-
-
activity in strain FL100
1.2e-05
-
-
pyridoxine 5'-phosphate activity in seedlings
1.78e-05
-
-
pyridoxine 5'-phosphate activity in root extracts
1.9e-05
-
-
pyridoxine 5'-phosphate activity in leaf extracts
2.2e-05
-
-
activity in crude extracts
2.5e-05
-
Chloridazon-degrading bacterium
-
activity in crude extracts
2.8e-05
-
-
activity in strain Al114
3.5e-05
-
-
pyridoxine 5'-phosphate activity in extracts of seedlings
3.66e-05
-
-
pyridoxine 5'-phosphate activity in mabikina extracts
4e-05
-
-
activity in crude extracts
4.2e-05
-
-
activity in crude extracts
6.5e-05
-
-
activity in suspension of cultered cells, substrate pyridoxamine 5'-phosphate; PMP oxidase activity in cell suspension culture
6.5e-05
-
-
activity in crude extracts
6.7e-05
-
-
activity in crude extracts, strain B
6.8e-05
-
-
activity in crude extracts
7e-05
-
-
PMP oxidase activity in callus culture
7.2e-05
-
-
activity in callus, substrate pyridoxamine 5'-phosphate
7.3e-05
-
-
pyridoxine 5'-phosphate activity in seedlings
7.3e-05
-
-
activity in crude extracts
7.45e-05
-
-
pyridoxine 5'-phosphate activity in extracts of seedlings
8e-05
-
-
activity in crude extracts
8.4e-05
-
-
pyridoxine 5'-phosphate activity in seedlings
8.5e-05
-
-
activity in crude extracts
9.7e-05
-
-
activity in cell suspension cultures, substrate pyridoxine 5'-phosphate
0.0001
-
-
activity in callus, substrate pyridoxine 5'-phosphate; PNP oxidase activity in callus culture and in cell suspension culture
0.00012
-
-
activity in seedlings, substrate pyridoxamine 5'-phosphate; PMP oxidase activity in seedlings
0.0005
-
-
activity in seedlings, substrate pyridoxine 5'-phosphate; PNP oxidase activity in seedlings
0.0005
-
-
activity in crude extracts
0.000667
-
-
activity in crude extracts
0.0007
-
-
activity in crude extracts
0.000717
-
-
activity in crude extracts, cells grown on minimal medium
0.0012
-
-
partialy purified enzyme
0.00188
-
-
isozyme EII
0.00367
-
-
isozyme EI
0.0417
-
-
activity of apoenzyme after dialysis of holoenzyme against potassium acetate buffer pH 4.0 and potassium phosphate buffer pH 7.0 for 24 h each
0.056
-
-
substrate pyridoxine 5'-phosphate, enzyme species FI which is assumed to be an artefact of the purification procedure
0.09
-
-
-
0.107
-
-
substrate pyridoxine 5'-phosphate, enzyme species FII
0.113
-
-
purified isozyme E-II, substrate pyridoxine 5'-phosphate
0.157
-
-
purified enzyme
0.293
-
-
recombinant enzyme
0.45
-
-
purified isozyme E-I, substrate pyridoxine 5'-phosphate
1.37
-
-
recombinant enzyme
additional information
-
-
development of a radiometric assay method, enzyme activity in erythrocytes and other tissues, overview
additional information
-
-
3.3 nmol/g hemoglobin/h, subject with a slow rate of pyridoxine conversion; 7.8 nmol/g hemoglobin/h, subject with a slow rate of pyridoxine conversion given 24 mg/day oral riboflavin for 2 weeks
additional information
-
-
25 nmol/g hemoglobin/h, activity in haemolysate
additional information
-
-
0.2 nmol/min*g fresh seedlings, activity in six-day old seedlings; 0.63 nmol/min*g fresh seedlings, activity in six-day-old seedlings after illumination with red light; quantification of activity during seed germination, overview
additional information
-
-
purified enzyme
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7
8
-
assay at
7.5
-
-
pyridoxine 5'-phosphate, immobilized enzyme
7.5
-
-
assay at
8
-
-
assay at
8
-
-
pyridoxine 5'-phosphate, soluble and immobilized enzyme
8
-
-
assay at
8
-
-
pyridoxine 5'-phosphate; soluble enzyme
8
-
-
assay at
8
-
-
assay at
8
-
-
pyridoxine 5'-phosphate
8.3
-
-
recombinant enzyme after cleavage from fusion protein
8.5
10
-
pyridoxamine phosphate oxidase activity remains nearly constant between pH 8.5 and 10.0
8.5
-
-
pyridoxine phosphate oxidase activity, slight optimum
9
10
-
pyridoxine 5'-phosphate, pyridoxamine 5'-phosphate
9
-
-
pyridoxamine 5'-phosphate, soluble enzyme
9
-
-
pyridoxamine 5'-phosphate, soluble and immobilized enzyme
9
-
-
in hemolysate
9
-
-
pyridoxamine 5'-phosphate
9
-
-, Q1PCB0
recombinant enzyme
9.5
-
-
immobilized enzyme, pyridoxamine 5'-phosphate
9.5
-
-
; both isozymes
11
-
-
assay at
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
10
-
pyridoxine phosphate oxidase activity
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
7
10.5
-, Q1PCB0
-
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
23
-
-
assay at
36
-
-
immobilized enzyme
37
-
-
assay at
37
-
-
assay at
37
-
-
assay at
37
-
-
asssay at
37
-
-
assay at
37
-
-
assay at
37
-
-, Q1PCB0
assay at
40
-
-
isozymes EI and EII, rapid decrease above
44
-
-
soluble enzyme
45
-
-
soluble enzyme
55
-
-
immobilized enzyme
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
50
-
immobilized enzyme at 25C: about 60% of maximal activity, soluble enzyme approx. 40%, immobilized enzyme at 50C: about 30% of maximal activity, soluble enzyme approx. 20%
30
55
-
at 30C: about 50% of maximal activity, at 55C: about 15% of maximal activity
38
60
-
at 38C: about 55% of maximal activity, at 60C: about 20% of maximal activity
additional information
-
-
rapid decrease in activity above 40C, both isozymes
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
-
the pI values of the isozymes differ from each other
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
0.7% of the activity in liver
Manually annotated by BRENDA team
-
11.5% of the activity in liver
Manually annotated by BRENDA team
-
13.0% of the activity in liver
Manually annotated by BRENDA team
-
1.2% of the activity in liver
Manually annotated by BRENDA team
-
14% of the activity in liver detected in left atrium, 11.6% of the activity in liver detected in tight atrium
Manually annotated by BRENDA team
-
6.8% of the activity in liver
Manually annotated by BRENDA team
-
11.2% of the activity in liver
Manually annotated by BRENDA team
-
23.8% of the activity in liver
Manually annotated by BRENDA team
-
cultured from immature embryos, effects of culture medium on enzyme activity in callus cultures
Manually annotated by BRENDA team
-
19.0% of the activity in liver
Manually annotated by BRENDA team
-
2.0% of the activity in liver
Manually annotated by BRENDA team
-
13.3% of the activity in liver detected in left cerebellum, 25.0% of the activity in liver detected in the right cerebellum
Manually annotated by BRENDA team
-
25.9% of the activity in liver
Manually annotated by BRENDA team
-
1.2% of the activity in liver detected in ascending colon, 7.9% of the activity in liver is detected in transverse colon, 2.8% of the activity in liver is detected in descending colon
Manually annotated by BRENDA team
-
5.1% of the activity in liver
Manually annotated by BRENDA team
-
18.4% of the activity in liver
Manually annotated by BRENDA team
-
1.1% of the activity in liver
Manually annotated by BRENDA team
-
9.3% of the activity in liver
Manually annotated by BRENDA team
-
7.5% of the activity in liver
Manually annotated by BRENDA team
-
lowest expression
Manually annotated by BRENDA team
-
12.4% of the activity in liver
Manually annotated by BRENDA team
-
3.7% of the activity in liver
Manually annotated by BRENDA team
-
3.5% of the activity in liver
Manually annotated by BRENDA team
-
12.3% of the activity in liver
Manually annotated by BRENDA team
-
PNPO immunoreactivities are significantly increased in the rat hippocampus accompanied by reductions in paired-pulse inhibition at 1 day and 1 week after status epilepticus
Manually annotated by BRENDA team
-
2.3% of the activity in liver
Manually annotated by BRENDA team
-
6.1% of the activity in liver
Manually annotated by BRENDA team
-
5.8% of the activity in liver
Manually annotated by BRENDA team
-
16.2% of the activity in liver
Manually annotated by BRENDA team
-
13.3% of the activity in liver
Manually annotated by BRENDA team
-
2.5% of the activity in liver
Manually annotated by BRENDA team
-
85.6% of the activity in liver
Manually annotated by BRENDA team
-
highest expression
Manually annotated by BRENDA team
-
4.1% of the activity in liver detected in the left ventricle
Manually annotated by BRENDA team
-
from peripheral blood, 0.4% of the activity in liver
Manually annotated by BRENDA team
-
30.2% of the activity of adult liver is detected in foetal liver
Manually annotated by BRENDA team
-
4.6% of the activity in liver
Manually annotated by BRENDA team
-
4.6% of the activity in liver
Manually annotated by BRENDA team
-
5.0% of the activity in liver
Manually annotated by BRENDA team
-
5.2% of the activity in liver
Manually annotated by BRENDA team
-
14.7% of the activity in liver
Manually annotated by BRENDA team
-
4.3% of the activity in liver
Manually annotated by BRENDA team
-
2.5% of the activity in liver
Manually annotated by BRENDA team
-
of cerebral cortex, 9.5% of the activity in liver
Manually annotated by BRENDA team
-
13.6% of the activity in liver
Manually annotated by BRENDA team
-
30.2% of the activity in liver
Manually annotated by BRENDA team
-
6.2% of the activity in liver
Manually annotated by BRENDA team
-
16.5% of the activity in liver
Manually annotated by BRENDA team
-
Cornu Ammonis 1 pyramidal cells
Manually annotated by BRENDA team
-
6.5% of the activity in liver
Manually annotated by BRENDA team
-
2.3% of the activity in liver
Manually annotated by BRENDA team
-
20.5% of the activity in liver detected in the right ventricle
Manually annotated by BRENDA team
-
10% of the activity in liver
Manually annotated by BRENDA team
-
change of activity during germination, overview
Manually annotated by BRENDA team
-
34.1% of the activity in liver
Manually annotated by BRENDA team
-
1.6% of the activity in liver
Manually annotated by BRENDA team
-
13.5% of the activity in liver
Manually annotated by BRENDA team
-
17.2% of the activity in liver
Manually annotated by BRENDA team
-
12.6% of the activity in liver
Manually annotated by BRENDA team
-
8.4% of the activity in liver
Manually annotated by BRENDA team
-
10.8% of the activity in liver
Manually annotated by BRENDA team
-
6.4% of the activity in liver
Manually annotated by BRENDA team
-
20.3% of the activity in liver
Manually annotated by BRENDA team
-
4.8% of the activity in liver
Manually annotated by BRENDA team
-
2.9% of the activity in liver
Manually annotated by BRENDA team
-
0.7% of the activity in liver
Manually annotated by BRENDA team
-
8.1% of the activity in liver
Manually annotated by BRENDA team
additional information
-
immunohistochemic analysis, overview
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
the enzyme contains an N-terminal chloroplast transit peptide
Manually annotated by BRENDA team
additional information
-
entirely present in 105000 x g supernatant fluid
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25500
-
-
recombinant enzyme after cleavage from fusion protein
27000
28000
-
gel filtration
31480
-
-
ESI-mass spectrometry
51000
-
-
gel filtration
51000
-
-
-
54000
-
-
gel filtration
55000
-
-
gel filtration
55000
-
-
analytical polyacrylamide disc gel electrophoresis
55380
-
-
nano-ESI mass spectroscopy
60000
-
-
polyacrylamide gradient gel electrophoresis
60000
-
-, Q1PCB0
recombinant enzyme, native PAGE
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 25000-28000, assumed to be a dimer, SDS-PAGE
?
-
x * 15000, recombinant detagged enzyme, SDS-PAGE
?
-
x * 49000, SDS-PAGE
?
Mycobacterium tuberculosis Rv2074
-
x * 15000, recombinant detagged enzyme, SDS-PAGE
-
dimer
-
2 * 30000, drastic denaturation conditions: 0.1% SDS and 2-mercaptoethanol, SDS-PAGE
dimer
-
2 * 27000, SDS-PAGE
dimer
-
1 * 27000 + 1 * 25000, SDS-PAGE
dimer
-
1 * 26762, deduced from nucleotide sequence
dimer
-
2 * 28000, SDS-PAGE
dimer
-, Q1PCB0
2 * 29000, recombinant enzyme, SDS-PAGE
homodimer
-
2 * 27000, SDS-PAGE
monomer
-
1 * 27000-28000, denaturing gel filtration
monomer
-
1 * 25500, recombinant enzyme after cleavage from fusion protein, gel filtration
additional information
-, O06553
structure modeling and analysis, overview
additional information
-
the enzyme contains an N-terminal chloroplast transit peptide, a long Yjef_N domain, and a C-terminal pyridox_oxidase domain
additional information
-, Q1PCB0
each monomer containing nine antiparallel beta-strands and five alpha-helical segments, secondary structure and three-dimensional structure, homology modelling, overview
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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
-
structures are defined at 2.0-2.1 A resolution
-
hanging-drop and sitting-drop method, crystallized without and with an excess of pyridoxal 5'-phosphate. Structures are determined to 1.95 A and 2.65 A, respectively
-
purified recombinant enzyme from strain Rv1155, sitting drop vapour diffusion method, 9 mg/ml enzyme in 50 mM Tris-HCl, pH 8.0, 25-50 mM KF, and 10 mM glutathione, mixed with an equal volume of precipitation solution containing 0.1 M HEPES, pH 7.5, 8% ethylene glycol, and 10% PEG 8000, macroseeding with hanging drops containing equal volumes of protein and precipitation solutions overnight prior to seeding, 1-2 weeks, cryoprotection by 30% ethylene glycol, X-ray diffraction structure determination and analysis at 1.7-2.2 A, modeling
-, O06553
purified recombinant enzyme from strain Rv2074, sitting drop vapour diffusion method in microtiter plates at room temperature, 12 mg/ml enzyme in 50 mM Tris-HCl, pH 8.0, 5 mM DTT, and glutathione, mixed with an equal volume of precipitation solution containing 0.2 M sodium citrate, pH 5.0, 30% glycerol, and 20% PEG 4000, hanging drop vapour diffusion with 0.5 ml protein and 1 ml precipitation solutions mixed, 1-2 weeks, cryoprotection by 30% glycerol, X-ray diffraction structure determination and analysis at 2.0 A, modeling
-
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.1
-
-
37C, 30 min, isozyme E I: 85% loss of activity, isozyme E II: 50% loss of activity
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5
-
-
pH 7.0, immobilized enzyme stable for 25 days, free enzyme: rapid loss of activity
24
-
-
pH 7.0, immobilized enzyme: 50% loss of activity after 10 days, free enzyme: 50% loss of activity after 2-3 days
25
-
-
half-life: 4 days immobilized enzyme, less than 1 day free enzyme
45
-
-
above 45C, loss of activity after 30 min
65
-
-
no loss in activity after incubation at temperatures below 50C, 30% to 40% activity loss after 15 min at 65C
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
bovine serum albumin stabilizes enzyme in dilute solution
-
repeated thawing and refreezing: denaturation
-
immobilized enzyme is more stable than purified free enzyme against heat and pH change
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-75C, 15% glycerol, several months, no loss in activity
-
4C, several weeks, no loss of activity
-
-20C, 18 months, over 80% of activity remains, apo- and holoenzyme
-
-20C, 4 years stable, shell-frozen apo- and holoenzyme
-
approx. 25C, immobilized enzyme, 200 mM K3PO4, pH 7.0, longer than 1 week
-
approx. 5C, immobilized enzyme, 200 mM K3PO4, pH 7.0, longer than 1 month
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
recombinant enzyme from Escherichia coli strain BL21 (DE3) to homogeneity
-, Q1PCB0
native enzyme with tightly bound FMN
-
recombinant enzyme, DEAE-cellulose, hydroxyapatite, CM-cellulose, Bio-Gel
-
Ni-NTA column chromatography
-
recombinant GST-tagged enzyme from Escherichia coli strain BL21(DE3) by glutathione affinity chromatography, removal of the GST-tag by rTEV protease, followed by dialysis and ultrafiltration
-, O06553
recombinant GST-tagged wild-type and of GST-tagged selenomethionine-labeled enzymes from Escherichia coli strain BL21(DE3) by glutathione affinity chromatography, removal of the GST-tags by rTEV protease, followed by dialysis and ultrafiltration
-
; native enzyme 556fold from liver by acid and ethanol precipitations, anion exchange chromatography, gel filtration, and calcium phosphate gel chromatography
-
acid treatment, ammonium sulfate, DEAE-Sephadex, Sephadex G-100, phosphopyridoxal-Sepharose
-
native enzyme from liver
-
affinity chromatography; native enzyme 3175fold from brain by pyridoxyl and phosphopyridoxyl affinity chromatography, gel filtration, and anion exchange chromatography, to homogeneity
-
affinity chromatography
-
native enzyme to homogeneity by calcium phosphate resin and anion exchange chromatography, and gel filtration, separation of isozymes PMP oxidase and PNP oxidase on calcium phosphate gel; partial
-
partially from 7-days-old seedlings, preparation of acetone powder
-
two isozymes from seedlings, partially by anion exchange and adsorption chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
gene AT5g49970, DNA and amino acid sequence determination and analysis, functional expression with and without N-terminal chloroplast transit peptide in Escherichia coli, functional complementation of a oxidation-sensitive Saccharomyces cerevisiae PDX3 knockout mutant
-
expressed in Escherichia coli
-
PNPO gene, DNA and amino acid sequence determination and analysis, genomic organization, expression in Escherichia coli strain BL21 (DE3)
-, Q1PCB0
expression in Escherichia coli
-
expression in Escherichia coli as maltose binding protein fusion
-
wild-type and mutant enzyme
-
expression in Escherichia coli
-
gene PNPO, DNA and amino acid sequence determination and analysis, expression of wild-type PNPO and mutant R229W in CHO cells
-
expressed in Escherichia coli BL21(DE3) cells
-
expression of GST-tagged wild-type and of GST-tagged selenomethionine-labeled enzymes from strain Rv2074 in Escherichia coli strain BL21(DE3)
-
expression of the GST-tagged enzyme from strain Rv1155 in Escherichia coli strain BL21(DE3)
-, O06553
expression in Escherichia coli
-
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
enzyme expression is down-regulated by exposure to drought (15%) and NaCl (43%). mRNA levels are also reduced by growth in the dark to 62%. Jasmonic acid treatment slightly decreases (20%) the level of mRNA after 8 h treatment
-
no substantial change in level occurs by exposure to UV irradiation
-
enzyme expression is up-regulated by light, heat shock (80% within 1 h), absicsic acid (43% after 4 h) and ethylene treatments (33% after 8 h)
-
PNPO immunoreactivities are significantly increased in the rat hippocampus accompanied by reductions in paired-pulse inhibition at 1 day and 1 week after status epilepticus
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
DELTA273-294
-
a deletion mutant lacking the C-terminal 22 amino acids shows that the C-terminus is essential for enzymatic activity
DELTAW294
-
a deletion mutant in which only the C-terminal tryptophan is deleted, displays activity similar to the wild type protein for chromophore and pyridoxal formation
D49A
-
decrease in affinity for pyridoxine 5'-phosphate
H199A
-
decrease in affinity for pyridoxine 5'-phosphate
H199N
-
little decrease in pyridoxine 5'-phosphate turnover
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
Y17F
-
decrease in affinity for pyridoxine 5'-phosphate
DELTA1-56
-
3.35fold increase in KM-value for pyridoxamine 5'-phosphate compared to wild-type enzyme, 2.95fold increase in KM-value for pyridoxine 5'-phosphate compared to wild-type enzyme, 6fold increase in KI-value for pyridoxal 5'-phosphate compared to wild-type enzyme
DELTA238-262
-
inactive mutant enzyme
R229W
-
the mutation is associated with lethality in neonatal epileptic encephalopathy
R95C
-
the mutation is associated with lethality in neonatal epileptic encephalopathy
R95H
-
the mutation is associated with lethality in neonatal epileptic encephalopathy
R229W
-
70% reduced activity compared to the wild-type enzyme, DNA sequence determination of PNPO homozygous missense, splice site and stop codon mutations involved in neonatal epileptic encephalopathy, phenotype overview
E50K
-
mutant shows activity similar to the wild-type enzyme
additional information
-
DNA sequence determination of PNPO homozygous missense, splice site and stop codon mutations involved in neonatal epileptic encephalopathy, phenotypes overview
Renatured/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
urea both activates and denatures the enzyme, reversible inactivation above 2.5 M, half-time of inactivation is 46 min at 2 M and 37C
-
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
analysis
-
pyridoxamine phosphate oxidase assay applicable for measuring activity in erythrocytes
synthesis
-
continuous production of pyridoxal 5'-phosphate with enzyme immobilized to iodo- and bromoacetyl polysaccharides