2.7.1.35: pyridoxal kinase
This is an abbreviated version!
For detailed information about pyridoxal kinase, go to the full flat file.
Word Map on EC 2.7.1.35
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2.7.1.35
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5'-phosphate
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vitamers
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pyridoxal-5'-phosphate
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plp-dependent
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4-pyridoxic
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ribokinase
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agriculture
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synthesis
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drug development
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medicine
- 2.7.1.35
- 5'-phosphate
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vitamers
- pyridoxal-5'-phosphate
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plp-dependent
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4-pyridoxic
- ribokinase
- agriculture
- synthesis
- drug development
- medicine
Reaction
Synonyms
ePL kinase, ePL kinase 1, hPL kinase, HPLK, kinase (phosphorylating), pyridoxal, kinase, pyridoxal (phosphorylating), LdPdxK, PdxK, pdxY, PKH, PL kinase, PLK, Plk1, PM kinase, PN kinase, PN/PL/PM kinase, pyridoxal 5-phosphate-kinase, pyridoxal kinase, pyridoxal kinase 1, pyridoxal kinase PKL, pyridoxal kinase-like protein SOS4, pyridoxal phosphokinase, pyridoxal/pyridoxine kinase, pyridoxamine kinase, pyridoxine kinase, pyridoxine/pyridoxal/pyridoxamine kinase, salt overly sensitive4, SAV0580, Sos4, StPLK, vitamin B6 kinase
ECTree
2.7.1.35 pyridoxal kinaseAdvanced search results
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results (Engineering
Engineering on EC 2.7.1.35 - pyridoxal kinase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
K229Q
A243G
naturally occuring mutation from a patient with diabetes, the mutant shows reduced catalytic activity and/or reduced affinity for PLP precursors, the mutant cannot complement the inactive Drosophila melanogaster dPdxk1 mutant when expressed in the mutant flies. Mutant A243G displays a damaging score of 0.72. The A243Q mutation somewhat reduces the affinity for ATP when using PL as substrate and the affinity for PM, while it does not affect KM for PL and PN. In addition, it has the effect to halve kcat with PL
D87H
naturally occuring mutation, the mutant shows reduced catalytic activity and/or reduced affinity for PLP precursors, the mutant cannot complement the inactive Drosophila melanogaster dPdxk1 mutant when expressed in the mutant flies. Mutant D87H displays the highest damaging score (1.0). The D87H mutation strongly increases KM for PL, and to a lesser extent also increases KM for PN and PM, leaving KM for ATP and kcat almost unaltered
H246Q
naturally occuring mutation, the mutant shows reduced catalytic activity and/or reduced affinity for PLP precursors, the mutant cannot complement the inactive Drosophila melanogaster dPdxk1 mutant when expressed in the mutant flies. Mutant H246Q displays a damaging score of 0.98. The H246Q mutation somewhat reduces the affinity for ATP when using PL as substrate and the affinity for PM, while it does not affect KM for PL and PN. In addition, it has the effect to halve kcat with PL
V128I
naturally occuring mutation, the mutant shows reduced catalytic activity and/or reduced affinity for PLP precursors, the mutant cannot complement the inactive Drosophila melanogaster dPdxk1 mutant when expressed in the mutant flies. Mutant V128I isplays a damaging score of 0.99. The V128I mutation drastically increases KM for PL and KM for ATP with this vitamer, whereas it does not affect kcat
D231A
site-directed mutagenesis of a GXGD motif residue, inactive mutant
G228A
site-directed mutagenesis of a GXGD motif residue, inactive mutant
G230A
site-directed mutagenesis of a GXGD motif residue, inactive mutant
T229A
site-directed mutagenesis of a GXGD motif residue, the mutation does not affect the catalytic function of enzyme LdPdxK, mutant T229A shows enzyme activity almost similar to wild-type LdPdxK. The Km value of T229A mutant for pyridoxal is 1.6fold reduced and the Km increased compared to wild-type
D231A
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site-directed mutagenesis of a GXGD motif residue, inactive mutant
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G228A
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site-directed mutagenesis of a GXGD motif residue, inactive mutant
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G230A
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site-directed mutagenesis of a GXGD motif residue, inactive mutant
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T229A
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site-directed mutagenesis of a GXGD motif residue, the mutation does not affect the catalytic function of enzyme LdPdxK, mutant T229A shows enzyme activity almost similar to wild-type LdPdxK. The Km value of T229A mutant for pyridoxal is 1.6fold reduced and the Km increased compared to wild-type
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C124A
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the mutant shows about 2fold increased catalytic efficiency compared to the wild type enzyme
C124A
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the mutant shows about 2fold increased catalytic efficiency compared to the wild type enzyme
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C110A
residue C110 is mandatory for pyridoxal, but not for pyridoxine, or 4-amino-5-hydroxymethyl-2-methylpyrimidine turnover
C214A
mutant does not turn over pyridoxal, pyridoxine, or 4-amino-5-hydroxymethyl-2-methylpyrimidine. Residue C214 acts as the catalytic base in the phosphorylation reaction
C110A
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residue C110 is mandatory for pyridoxal, but not for pyridoxine, or 4-amino-5-hydroxymethyl-2-methylpyrimidine turnover
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C214A
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mutant does not turn over pyridoxal, pyridoxine, or 4-amino-5-hydroxymethyl-2-methylpyrimidine. Residue C214 acts as the catalytic base in the phosphorylation reaction
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additional information
additional information
plants lacking enzyme activity display chlorosis and reduced plant size, and hypersensitivity to NaCl and sucrose. Mutant has higher level of pyridoxine, pyridoxamine, and pyridoxal 5'-phosphate. Mutant shows higher activity of pyridoxine/pyridoxamine 5'-phosphate oxidase as well as of the vitamin B6 de novo pathway enzyme Pdx1 and increased total vitamin B6 levels
additional information
in Drosophila, mutations in the dPdxk gene cause chromosome aberrations (CABs) and increased glucose content in larval hemolymph. The hyperglycemia phenotype is rescued by the expression of wild-type human PDXK enzyme, although not by human PDXK mutants D87H, V128I, H246Q, and A243G. To introduce the transgenes carrying the PDXK variants (PDXK VAR) in a mutant dPdxk1 background, the PDXKVAR/CyGFP, MKRS/TM6B females to CyGFP/Sco, dPdxk1/TM6B males are crossed. The progeny of this cross, PDXKVAR /CyGFP, dPdxk1/TM6B, is crossed inter se to obtain a stable stock
