Information on EC 1.4.3.5 - pyridoxal 5'-phosphate synthase

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

EC NUMBER
COMMENTARY hide
1.4.3.5
-
RECOMMENDED NAME
GeneOntology No.
pyridoxal 5'-phosphate synthase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
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 TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Deamination
-
-
-
-
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
4-amino-2-methyl-5-diphosphomethylpyrimidine biosynthesis (yeast)
-
-
pyridoxal 5'-phosphate biosynthesis I
-
-
pyridoxal 5'-phosphate salvage I
-
-
pyridoxal 5'-phosphate salvage II (plants)
-
-
vitamin B6 metabolism
-
-
Vitamin B6 metabolism
-
-
Metabolic pathways
-
-
Microbial metabolism in diverse environments
-
-
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 hide
9029-21-4
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
single copy PNPO gene
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Chloridazon-degrading bacterium
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
CB6
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
gene PNPO
-
-
Manually annotated by BRENDA team
-
UniProt
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
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
CBS 4
-
-
Manually annotated by BRENDA team
CBS 4
-
-
Manually annotated by BRENDA team
Japanese radish
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
-
an RNAi mutant shows sensitivity to high light
physiological function
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
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
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-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-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-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
-
-
-
?
epsilon-pyridoxyllysine 5'-phosphate + H2O + O2
pyridoxal 5'-phosphate + lysine + 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
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 + H2O + O2
pyridoxal 5'-phosphate + NH3 + H2O2
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 + O2
pyridoxal 5'-phosphate + H2O2
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
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 + H2O + O2
pyridoxal 5'-phosphate + NH3 + H2O2
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 + O2
pyridoxal 5'-phosphate + H2O2
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
specific for flavin-phosphate
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ammonium
-
in culture medium, activates PMP oxidase activity in callus culture by about 30%, no activation of PNP oxidase
potassium nitrate
-
in culture medium, activates PNP oxidase activity 2fold in callus culture, no activation of PMP oxidase
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
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
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
citrate-phosphate buffer
-
-
-
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
Phenylglyoxal
-
pyridoxal 5'-phosphate protects
pyridoxal 5'-phosphate
pyridoxal 5'-phosphate oxime
-
-
pyridoxaloxime 5'-phosphate
pyridoxamine 5'-phosphate
-
substrate inhibition above 0.0006 mM
pyridoxine 5'-phosphate
Urea
-
both activates and denatures the enzyme, reversible inactivation above 2.5 M, half-time of inactivation is 46 min at 2 M and 37°C
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
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
guanidine hydrochloride urea
-
both activates and denatures the enzyme
Tris
-
activation
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
additional information
-
the enzyme is induced by light without affecting the substrate specificity
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0059
5'-homopyridoxine-phosphate
-
-
0.0059 - 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
-
-
0.000016 - 0.000031
FMN
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 - 0.182
O2
0.035
Phospho-pyridoxyl-3-alanine
-
-
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 - 1
pyridoxamine 5'-phosphate
0.1
pyridoxamine-5'-phosphate
-
-
0.0003 - 2.4
pyridoxine 5'-phosphate
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
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
-
-
0.004
5'-phospho-pyridoxyl-p-aminophenol
-
-
33
pyridoxal 5'-phosphate
-
recombinant enzyme after cleavage from fusion protein
0.009 - 28
pyridoxamine 5'-phosphate
0.0002 - 0.76
pyridoxine 5'-phosphate
additional information
additional information
-
turnover numbers of mutant enzymes H199A, H199N, R197E, R197M, Y17F, R14E, R14M
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.028 - 29
pyridoxine 5'-phosphate
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0018 - 0.105
4'-deoxypyridoxine-5'-phosphate
0.003 - 23
pyridoxal 5'-phosphate
0.002
pyridoxal 5'-phosphate oxime
-
-
0.05
pyridoxine 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]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.00000062
-
pyridoxine 5'-phosphate activity in seedlings
0.000001
-
pyridoxine 5'-phosphate activity in seedlings
0.0000012
-
pyridoxine 5'-phosphate activity in root extracts
0.0000013
0.0000015
-
pyridoxine 5'-phosphate activity in seedlings
0.0000043
-
activity in strain FL100
0.000012
-
pyridoxine 5'-phosphate activity in seedlings
0.0000178
-
pyridoxine 5'-phosphate activity in root extracts
0.000019
-
pyridoxine 5'-phosphate activity in leaf extracts
0.000022
-
activity in crude extracts
0.000025
Chloridazon-degrading bacterium
-
activity in crude extracts
0.000028
-
activity in strain Al114
0.000035
-
pyridoxine 5'-phosphate activity in extracts of seedlings
0.0000366
-
pyridoxine 5'-phosphate activity in mabikina extracts
0.00004
-
activity in crude extracts
0.000042
-
activity in crude extracts
0.000065
0.000067
-
activity in crude extracts, strain B
0.000068
-
activity in crude extracts
0.00007
-
PMP oxidase activity in callus culture
0.000072
-
activity in callus, substrate pyridoxamine 5'-phosphate
0.000073
0.0000745
-
pyridoxine 5'-phosphate activity in extracts of seedlings
0.00008
-
activity in crude extracts
0.000084
-
pyridoxine 5'-phosphate activity in seedlings
0.000085
-
activity in crude extracts
0.000097
-
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
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
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 8
-
assay at
8.3
-
recombinant enzyme after cleavage from fusion protein
8.5
-
pyridoxine phosphate oxidase activity, slight optimum
8.5 - 10
-
pyridoxamine phosphate oxidase activity remains nearly constant between pH 8.5 and 10.0
9 - 10
-
pyridoxine 5'-phosphate, pyridoxamine 5'-phosphate
11
-
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
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
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
23
-
assay at
36
-
immobilized enzyme
40
-
isozymes EI and EII, rapid decrease above
44
-
soluble enzyme
55
-
immobilized enzyme
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 50
-
immobilized enzyme at 25°C: about 60% of maximal activity, soluble enzyme approx. 40%, immobilized enzyme at 50°C: about 30% of maximal activity, soluble enzyme approx. 20%
30 - 55
-
at 30°C: about 50% of maximal activity, at 55°C: about 15% of maximal activity
38 - 60
-
at 38°C: about 55% of maximal activity, at 60°C: about 20% of maximal activity
additional information
-
rapid decrease in activity above 40°C, both isozymes
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
the pI values of the isozymes differ from each other
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
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
-
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
-
of cerebral cortex, 9.5% 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
-
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
-
3.5% of the activity in liver
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
-
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
-
4.6% of the activity in liver
Manually annotated by BRENDA team
-
5.0% of the activity in liver
Manually annotated by BRENDA team
-
8.1% 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
-
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
-
17.2% of the activity in liver
Manually annotated by BRENDA team
-
5.1% 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
additional information
-
immunohistochemic analysis, overview
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
-
entirely present in 105000 x g supernatant fluid
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
UNIPROT
ORGANISM
Burkholderia lata (strain ATCC 17760 / DSM 23089 / LMG 22485 / NCIMB 9086 / R18194 / 383);
Escherichia coli (strain K12);
Homo sapiens;
A0R6F1
Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155);
P9WIJ1
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv);
P38075
Saccharomyces cerevisiae (strain ATCC 204508 / S288c);
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
15000
-
x * 15000, recombinant detagged enzyme, SDS-PAGE
25000
-
1 * 27000 + 1 * 25000, SDS-PAGE
25500
-
recombinant enzyme after cleavage from fusion protein
26762
-
1 * 26762, deduced from nucleotide sequence
27000 - 28000
-
gel filtration
28000
-
2 * 28000, SDS-PAGE
29000
2 * 29000, recombinant enzyme, SDS-PAGE
30000
-
2 * 30000, drastic denaturation conditions: 0.1% SDS and 2-mercaptoethanol, SDS-PAGE
31480
-
ESI-mass spectrometry
49000
-
x * 49000, SDS-PAGE
54000
-
gel filtration
55380
-
nano-ESI mass spectroscopy
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
monomer
additional information
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
-
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
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
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.1
-
37°C, 30 min, isozyme E I: 85% loss of activity, isozyme E II: 50% loss of activity
391881
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
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 45°C, loss of activity after 30 min
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
acetylation leads to a decrease of the enzymatic activity
-
bovine serum albumin stabilizes enzyme in dilute solution
-
immobilized enzyme is more stable than purified free enzyme against heat and pH change
-
repeated thawing and refreezing: denaturation
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 18 months, over 80% of activity remains, apo- and holoenzyme
-
-20°C, 4 years stable, shell-frozen apo- and holoenzyme
-
-75°C, 15% glycerol, several months, no loss in activity
-
4°C, several weeks, no loss of activity
-
approx. 25°C, immobilized enzyme, 200 mM K3PO4, pH 7.0, longer than 1 week
-
approx. 5°C, immobilized enzyme, 200 mM K3PO4, pH 7.0, longer than 1 month
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
; 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
-
affinity chromatography
-
affinity chromatography; native enzyme 3175fold from brain by pyridoxyl and phosphopyridoxyl affinity chromatography, gel filtration, and anion exchange chromatography, to homogeneity
-
His Trap column chromatography and Superdex 200 gel filtration
-
HisTrap nickel-affinity column chromatography and Superdex 200 gel filtration
native enzyme from liver
-
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
-
native enzyme with tightly bound FMN
-
Ni-NTA column chromatography
-
nickel affinity column chromatography
-
partial
partially from 7-days-old seedlings, preparation of acetone powder
-
recombinant enzyme from Escherichia coli strain BL21 (DE3) to homogeneity
recombinant enzyme, DEAE-cellulose, hydroxyapatite, CM-cellulose, Bio-Gel
-
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
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
-
two isozymes from seedlings, partially by anion exchange and adsorption chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
-
expressed in Escherichia coli BL21 DE3 Rosetta cells
-
expressed in Escherichia coli BL21(DE3) cells
expression in Escherichia coli
expression in Escherichia coli as maltose binding protein fusion
-
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)
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
-
gene PNPO, DNA and amino acid sequence determination and analysis, expression of wild-type PNPO and mutant R229W in CHO cells
-
PNPO gene, DNA and amino acid sequence determination and analysis, genomic organization, expression in Escherichia coli strain BL21 (DE3)
wild-type and mutant enzyme
-
EXPRESSION
ORGANISM
UNIPROT
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
-
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)
-
no substantial change in level occurs by exposure to UV irradiation
-
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
COMMENTARY hide
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
K159Q
-
the mutation has no effect on the catalytic activity
K159R
-
the mutation has no effect on the catalytic activity
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
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
R95H
-
the mutation is associated with lethality in neonatal epileptic encephalopathy
E50K
-
mutant shows activity similar to the wild-type enzyme
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
additional information
-
DNA sequence determination of PNPO homozygous missense, splice site and stop codon mutations involved in neonatal epileptic encephalopathy, phenotypes overview