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
-
vitamers
-
pyridoxal-5'-phosphate
-
plp-dependent
-
4-pyridoxic
-
ribokinase
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agriculture
-
synthesis
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drug development
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medicine
- 2.7.1.35
- 5'-phosphate
-
vitamers
- pyridoxal-5'-phosphate
-
plp-dependent
-
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 (Substrates Products
Substrates Products on EC 2.7.1.35 - pyridoxal kinase
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + 4'-O-methylpyridoxine
ADP + 4'-O-methylpyridoxine 5'-phosphate
-
-
-
?
ATP + 4-amino-5-hydroxymethyl-2-methylpyrimidine
ADP + 4-amino-5-phosphomethyl-2-methylpyrimidine
ATP + methyl (1S)-1-[3-hydroxy-5-(hydroxymethyl)-2-methylpyridin-4-yl]-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxylate
ADP + methyl (1S)-1-[3-hydroxy-5-(hydroxymethyl)-2-methylpyridin-4-yl]-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxylate 5'-phosphate
-
-
-
?
ATP + methyl N-[[3-hydroxy-5-(hydroxymethyl)-2-methylpyridin-4-yl]methyl]histidinate
ADP + methyl N-[[3-hydroxy-5-(hydroxymethyl)-2-methylpyridin-4-yl]methyl]histidinate 5'-phosphate
-
-
-
?
ATP + methyl N-[[3-hydroxy-5-(hydroxymethyl)-2-methylpyridin-4-yl]methyl]tryptophanate
ADP + methyl N-[[3-hydroxy-5-(hydroxymethyl)-2-methylpyridin-4-yl]methyl]tryptophanate 5'-phosphate
-
-
-
?
methyl (1S)-1-[3-hydroxy-5-(hydroxymethyl)-2-methylpyridin-4-yl]-2,3,4,9-tetrahydro-1H-beta-carboline-3-carboxylate + ATP
methyl (1S)-1-[3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl]-2,3,4,9-tetrahydro-1H-beta-carboline-3-carboxylate + ADP
-
-
very probably: methyl (1S)-1-[3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl]-2,3,4,9-tetrahydro-1H-beta-carboline-3-carboxylate is an inhibitor of Plasmodium falciparum ornithine decarboxylase
-
?
methyl N-[[3-hydroxy-5-(hydroxymethyl)-2-methylpyridin-4-yl]methyl]histidinate + ATP
methyl N-([3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl]methyl)histidinate + ADP
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-
methyl N-([3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl]methyl)histidinate is an inhibitor of Plasmodium falciparum ornithine decarboxylase: IC50 = 0.058 mM
-
?
methyl N-[[3-hydroxy-5-(hydroxymethyl)-2-methylpyridin-4-yl]methyl]tryptophanate + ATP
methyl N-([3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl]methyl)tryptophanate + ADP
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-
methyl N-([3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]pyridin-4-yl]methyl)tryptophanate is an inhibitor of Plasmodium falciparum ornithine decarboxylase: IC50 = 0.064 mM
-
?
ATP + 4-amino-5-hydroxymethyl-2-methylpyrimidine
ADP + 4-amino-5-phosphomethyl-2-methylpyrimidine
-
-
-
-
?
ATP + 4-amino-5-hydroxymethyl-2-methylpyrimidine
ADP + 4-amino-5-phosphomethyl-2-methylpyrimidine
reaction of EC 2.7.1.49
-
-
?
ATP + 4-amino-5-hydroxymethyl-2-methylpyrimidine
ADP + 4-amino-5-phosphomethyl-2-methylpyrimidine
reaction of EC 2.7.1.49
-
-
?
ATP + 4-deoxypyridoxine
ADP + 4-deoxypyridoxine 5'-phosphate
-
-
-
-
?
ATP + 4-deoxypyridoxine
ADP + 4-deoxypyridoxine 5'-phosphate
-
-
-
-
?
ATP + ginkgotoxin
?
ginkgotoxin (from leaves of Ginkgo biloba) acts as pseudo-substrate for pyridoxal kinase with a Km value of 0.0297 mM
-
-
?
ATP + ginkgotoxin
?
ginkgotoxin (from leaves of Ginkgo biloba) acts as pseudo-substrate for pyridoxal kinase with a Km value of 0.0297 mM
-
-
?
ATP + omega-methylpyridoxal
ADP + omega-methylpyridoxal 5'-phosphate
-
-
-
-
?
ATP + omega-methylpyridoxal
ADP + omega-methylpyridoxal 5'-phosphate
-
-
-
-
?
ATP + omega-methylpyridoxal
ADP + omega-methylpyridoxal 5'-phosphate
-
-
-
-
?
ATP + omega-methylpyridoxal
ADP + omega-methylpyridoxal 5'-phosphate
-
-
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
-
the SOS4 gene encodes a pyridoxal kinase that functions upstream of ethylene and auxin in root hair development, SOS4 is required for the initiation and tip growth of root hairs
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
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generates the active form of vitamin B6, which serves as cofactor for many enzymes
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-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
-
the pdxY gene encodes a novel pyridoxal kinase involved in the salvage pathway of pyridoxal 5'-phosphate biosynthesis. The pyridoxal kinase PdxY and the pyridoxine/pyridoxal/pyridoxamine kinase PdxK are the only physiologically important B6 vitamer kinases in Escherichia coli and their function is confined to the pyridoxal 5'-phosphate salvage pathway
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-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
-
generates the active form of vitamin B6, which serves as cofactor for many enzymes
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
generates the active form of vitamin B6, which serves as cofactor for many enzymes
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
-
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
-
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
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generates the active form of vitamin B6, which serves as cofactor for many enzymes, increased enzyme activity detected 12-24 h after ischemia, pyridoxal 5'-phosphate essential for the synthesis of some neurotransmitters
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-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
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key enzyme in transformation of vitamin B6 to pyridoxal 5'-phosphate. Pyridoxal 5'-phosphate is the crucial cofactor required by numerous enzymes involved in the metabolism of amino acids and the synthesis of many neurotransmitters
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-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
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generates the active form of vitamin B6, which serves as cofactor for many enzymes
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-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
generates the active form of vitamin B6, which serves as cofactor for many enzymes
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
-
generates the active form of vitamin B6, which serves as cofactor for many enzymes
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
-
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
preferred substrate
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-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
-
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
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important enzyme involved in bioactivation of vitamin B6
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-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
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generates the active form of vitamin B6, which serves as cofactor for many enzymes, interaction of pyridoxal kinase with pyridoxal 5'-phosphate dependent enzymes seems to be important for providing sufficient amounts of enzyme cofactor
-
-
?
ATP + pyridoxamine
ADP + pyridoxamine 5'-phosphate
-
-
-
?
ATP + pyridoxamine
ADP + pyridoxamine 5'-phosphate
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33% of the activity with pyridoxal
-
-
?
ATP + pyridoxamine
ADP + pyridoxamine 5'-phosphate
-
-
-
?
ATP + pyridoxamine
ADP + pyridoxamine 5'-phosphate
-
not a substrate of the purified enzyme
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-
?
ATP + pyridoxamine
ADP + pyridoxamine 5'-phosphate
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study of substrate-enzyme interaction between immobilized pyridoxamine and recombinant porcine pyridoxal kinase using surface plasmon resonance biosensor
-
-
?
ATP + pyridoxine
ADP + pyridoxine 5'-phosphate
-
-
-
?
ATP + pyridoxine
ADP + pyridoxine 5'-phosphate
-
40% of the activity with pyridoxal
-
-
?
ATP + pyridoxine
ADP + pyridoxine 5'-phosphate
-
-
-
?
ATP + pyridoxine
ADP + pyridoxine 5'-phosphate
-
46% of the activity with pyridoxal
-
-
?
additional information
?
-
-
the enzyme possesses also a 4-amino-5-hydroxymethyl-2-methylpyrimidine kinase activity
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-
?
additional information
?
-
pyridoxal kinase catalyzes the forward reactions with pyridoxal, pyridoxamine, and pyridoxine, while pyridoxal phosphotase (PL phosphatase, PDXP, EC 3.1.3.74) catalyzes the reverse reaction of dephophorylation
-
-
-
additional information
?
-
-
pyridoxal kinase catalyzes the forward reactions with pyridoxal, pyridoxamine, and pyridoxine, while pyridoxal phosphotase (PL phosphatase, PDXP, EC 3.1.3.74) catalyzes the reverse reaction of dephophorylation
-
-
-
additional information
?
-
docking analysis of potent antimalarials to the enzyme, molecular docking indicates potential binding modes of methyl (1S)-1-[3-hydroxy-5-(hydroxymethyl)-2-methylpyridin-4-yl]-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxylate, methyl N-[[3-hydroxy-5-(hydroxymethyl)-2-methylpyridin-4-yl]methyl]tryptophanate, and methyl N-[[3-hydroxy-5-(hydroxymethyl)-2-methylpyridin-4-yl]methyl]histidinate as substrates of PfPdxK. PfPdxK is strongly implicated in the phosphorylation of methyl (1S)-1-[3-hydroxy-5-(hydroxymethyl)-2-methylpyridin-4-yl]-2,3,4,9-tetrahydro-1H-pyrido[3,4-b]indole-3-carboxylate, methyl N-[[3-hydroxy-5-(hydroxymethyl)-2-methylpyridin-4-yl]methyl]tryptophanate, and methyl N-[[3-hydroxy-5-(hydroxymethyl)-2-methylpyridin-4-yl]methyl]histidinate into their active forms
-
-
-
additional information
?
-
substrate binding strutures analysis from cyrstal structure of the enzyme-ligand complex, overview. ATP is covalently attached to Lys233 via a Schiff base linkage. In StPLK, the alpha-phosphate of ADP interacts with Ser201, Thr235, and nearby water molecule. The beta-phosphate of ADP interacts with Gly236, Asn164, one Mg2+ ion, and a few water molecules. Pyridoxal is covalently attached to an active site lysine residue (Lys233) forming a Schiff base, as well as to ADP, and a Mg2+ ion. Active site structure. Structure comparisons with other pyridoxal kinases from other species
-
-
-
additional information
?
-
the reactive Cys110 residue in the lid region forms a hemithioactetal intermediate with the 4'-aldehyde of pyridoxal. This hemithioacetal, in concert with the catalytic Cys214, increases the nucleophilicity of the pyridoxal 5'-OH group for the inline displacement reaction with the gamma-phosphate of ATP
-
-
?
additional information
?
-
-
the reactive Cys110 residue in the lid region forms a hemithioactetal intermediate with the 4'-aldehyde of pyridoxal. This hemithioacetal, in concert with the catalytic Cys214, increases the nucleophilicity of the pyridoxal 5'-OH group for the inline displacement reaction with the gamma-phosphate of ATP
-
-
?
additional information
?
-
the reactive Cys110 residue in the lid region forms a hemithioactetal intermediate with the 4'-aldehyde of pyridoxal. This hemithioacetal, in concert with the catalytic Cys214, increases the nucleophilicity of the pyridoxal 5'-OH group for the inline displacement reaction with the gamma-phosphate of ATP
-
-
?
