Information on EC 1.4.3.5 - pyridoxal 5'-phosphate synthase

New: Word Map on EC 1.4.3.5
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:
Search Reference ID:
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 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)
-
-
Metabolic pathways
-
-
Microbial metabolism in diverse environments
-
-
pyridoxal 5'-phosphate biosynthesis I
-
-
pyridoxal 5'-phosphate salvage I
-
-
pyridoxal 5'-phosphate salvage II (plants)
-
-
vitamin B6 metabolism
-
-
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.
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
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
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
-
-
-
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 37C
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
0.031
5'-methylpyridoxine-phosphate
-
-
0.025
5'-phospho-pyridoxal-O-carboxymethyloxime
-
-
0.021
5'-phospho-pyridoxaloxime
-
-
0.01
5'-phospho-pyridoxyl-3-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
0.035
5'-phospho-pyridoxyl-5-aminovalerate
Sus scrofa
-
-
0.01
5'-phospho-pyridoxyl-aniline
Sus scrofa
-
-
0.1
5'-phospho-pyridoxyl-m-aminobenzoate
0.004
5'-phospho-pyridoxyl-p-aminophenol
Sus scrofa
-
-
33
pyridoxal 5'-phosphate
Escherichia coli
-
recombinant enzyme after cleavage from fusion protein
0.009 - 28
pyridoxamine 5'-phosphate
0.008 - 0.76
pyridoxine 5'-phosphate
additional information
additional information
Escherichia coli
-
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
pyridoxine 5'-phosphate
Mycobacterium tuberculosis
-
in 25 mM potassium phosphate, pH 7.8 and 25C
1037
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 - 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
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
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 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
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
ORGANISM
UNIPROT
Burkholderia lata (strain ATCC 17760 / LMG 22485 / NCIMB 9086 / R18194 / 383)
Burkholderia lata (strain ATCC 17760 / LMG 22485 / NCIMB 9086 / R18194 / 383)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Streptococcus suis (strain 89/1591)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25500
-
recombinant enzyme after cleavage from fusion protein
27000 - 28000
-
gel filtration
31480
-
ESI-mass spectrometry
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
-
37C, 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 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
LITERATURE
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
-20C, 18 months, over 80% of activity remains, apo- and holoenzyme
-
-20C, 4 years stable, shell-frozen apo- and holoenzyme
-
-75C, 15% glycerol, several months, no loss in activity
-
4C, several weeks, no loss of activity
-
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
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
-
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
-
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) 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
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
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
Renatured/COMMENTARY
ORGANISM
UNIPROT
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
COMMENTARY hide
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
Show AA Sequence (5786 entries)
Longer loading times are possible. Please use the Sequence Search for a certain query.