1.4.3.5: pyridoxal 5'-phosphate synthase
This is an abbreviated version!
For detailed information about pyridoxal 5'-phosphate synthase, go to the full flat file.
Word Map on EC 1.4.3.5
Reaction
Synonyms
ePNPOx, FprA protein, oxidase, pyridoxamine phosphate, Pdx1, PDX3, PdxH, PMP oxidase, PNP oxidase, PNP/PMP oxidase, PNPO, PNPOx, PPOX, pyridox(am)ine 5'-phosphate oxidase, pyridoxal 5'-phosphate synthase, pyridoxal 5'-phosphate synthetic enzyme, pyridoxamine (pyridoxine) 5'-phosphate oxidase, pyridoxamine (pyridoxine) 5’-phosphate:O2 oxidoreductase (deaminating), pyridoxamine 5'-phosphate oxidase, pyridoxamine phosphate oxidase, pyridoxamine-5-phosphate oxidase, pyridoxamine-phosphate oxidase, pyridoxaminephosphate oxidase (EC 1.4.3.5: deaminating), pyridoxinamine 5'-phosphate oxidase, pyridoxine (pyridoxamine) 5 '-phosphate oxidase, pyridoxine (pyridoxamine) 5'-phosphate oxidase, pyridoxine (pyridoxamine) phosphate oxidase, pyridoxine 5'-phosphate oxidase, pyridoxine 5'-phosphate oxidase`, pyridoxine 5-phosphate oxidase, pyridoxine phosphate oxidase, pyridoxine-5'-phosphate oxidase, pyridoxine/pyridoxamine 5'-phosphate oxidase, pyridoxine/pyridoxamine phosphate oxidase, sgll, Sgll/PNPO, Ylr456w, Ypr172w
ECTree
1.4.3.5 pyridoxal 5'-phosphate synthaseAdvanced search results
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results (Engineering
Engineering on EC 1.4.3.5 - pyridoxal 5'-phosphate synthase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
DELTA273-294
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a deletion mutant lacking the C-terminal 22 amino acids shows that the C-terminus is essential for enzymatic activity
DELTAW294
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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
K145A/F177A
the Tm-value is about 1°C higher than the Tm-value of the wild-type enzyme
K72A
-
the mutant shows a sharp decrease of the catalytic activity compared to the wild type enzyme
K72P
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the mutant shows a sharp decrease of the catalytic activity compared to the wild type enzyme
K72Q
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the mutant shows a sharp decrease of the catalytic activity compared to the wild type enzyme
K72R
-
the mutant shows a slight decrease of the catalytic activity compared to the wild type enzyme
N84A/K145A/F177A
the Tm-value is about 3.3°C lower than the Tm-value of the wild-type enzyme
N84W/K145A/F177A
the Tm-value is about 3.4°C lower than the Tm-value of the wild-type enzyme
R197M
catalyzes removal of the proS hydrogen atom from (4'R)-3H-pyridoxamine 5'-phosphate, decrease in affinity for pyridoxine 5'-phosphate
R215L
the Tm-value is 1°C lower than the Tm-value of the wild-type enzyme
R23L
the Tm-value is identical to the Tm-value of the wild-type enzyme
R23L/R24L/R21L
complete loss of allosteric properties. The Tm-value is about 2°C lower than the Tm-value of the wild-type enzyme
K145A/F177A
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the Tm-value is about 1°C higher than the Tm-value of the wild-type enzyme
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R23L/R24L/R21L
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complete loss of allosteric properties. The Tm-value is about 2°C lower than the Tm-value of the wild-type enzyme
-
DELTA1-56
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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
G118R
pathogenic variant that is responsible for pyridoxamine 5'-phosphate oxidase deficiency. 51% of the activity as compared to wild-type enzyme. Tm-value of the mutant enzyme (in absence and presence of FMN) is about 10°C lower than the Tm-value of the wilde-type enzyme
R116Q
R116Q/R225H
pathogenic variant that is responsible for pyridoxamine 5'-phosphate oxidase deficiency. The Tm-value of the mutant enzyme in absence of FMN is 5.3°C lower than the Tm-value of the wilde-type enzyme in absence of FMN. The Tm-value of the mutant enzyme in absence of FMN is 4.7°C lower than the Tm-value of the wilde-type enzyme in presence of FMN
R118Q
later onset of symptoms of severe encephalopathy (beyond the first months of life) and peculiar epileptic manifestations in patients
R141C
pathogenic variant that is responsible for pyridoxamine 5'-phosphate oxidase deficiency. The Tm-value of the mutant enzyme in absence of FMN is 6.2°C lower than the Tm-value of the wilde-type enzyme in absence of FMN. The Tm-value of the mutant enzyme in absence of FMN is 6.0°C lower than the Tm-value of the wilde-type enzyme in presence of FMN
R225H
pathogenic variant that is responsible for pyridoxamine 5'-phosphate oxidase deficiency. The Tm-value of the mutant enzyme in absence of FMN is 5.1°C higher than the Tm-value of the wilde-type enzyme in absence of FMN. The Tm-value of the mutant enzyme in absence of FMN is 3.8°C lower than the Tm-value of the wilde-type enzyme in presence of FMN
R229W
R95C
R95H
-
the mutation is associated with lethality in neonatal epileptic encephalopathy
X262Q
pathogenic variant that is responsible for pyridoxamine 5'-phosphate oxidase deficiency. The Tm-value of the mutant enzyme in absence of FMN is 2.7°C lower than the Tm-value of the wilde-type enzyme in absence of FMN. The Tm-value of the mutant enzyme in absence of FMN is 4.7°C lower than the Tm-value of the wilde-type enzyme in presence of FMN
R229W
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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
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DNA sequence determination of PNPO homozygous missense, splice site and stop codon mutations involved in neonatal epileptic encephalopathy, phenotypes overview
R116Q
the Tm-value of the mutant enzyme in absence of FMN is 7.2°C lower than the Tm-value of the wilde-type enzyme in absence of FMN. The Tm-value of the mutant enzyme in absence of FMN is 8.2°C lower than the Tm-value of the wilde-type enzyme in presence of FMN
R229W
-
the mutation is associated with lethality in neonatal epileptic encephalopathy
R229W
the mutation leads to deficiency of pyridoxal 5'-phosphate in the cell and causes neonatal epileptic encephalopathy
R95C
-
the mutation is associated with lethality in neonatal epileptic encephalopathy
R95C
the mutation leads to deficiency of pyridoxal 5'-phosphate in the cell and causes neonatal epileptic encephalopathy. The mutant exhibits a 15fold reduction in affinity for the FMN cofactor, a 71fold decrease in affinity for the substrate pyridoxine 5'-phosphate, a 4.9fold decrease in specific activity, and a 343fold reduction in catalytic activity, compared to the wild type enzyme
