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ATP + 4'-deoxypyridoxine
ADP + 4'-deoxypyridoxine 5'-phosphate
-
-
-
?
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 + 4-deoxypyridoxine
ADP + 4-deoxypyridoxine 5'-phosphate
ATP + 5-deoxypyridoxal
ADP + ?
ATP + ginkgotoxin
ADP + ginkgotoxin 5'-phosphate
-
-
-
?
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
-
-
-
?
ATP + omega-methylpyridoxal
ADP + omega-methylpyridoxal 5'-phosphate
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
ATP + pyridoxamine
ADP + pyridoxamine 5'-phosphate
ATP + pyridoxine
ADP + pyridoxine 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
-
-
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
-
-
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
-
?
pyridoxal + ATP
pyridoxal 5'-phosphate + ADP
pyridoxamine + ATP
pyridoxamine 5'-phosphate
-
-
-
-
?
pyridoxine + ATP
pyridoxine 5'-phosphate
-
-
-
-
?
additional information
?
-
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 + 4-deoxypyridoxine
ADP + 4-deoxypyridoxine 5'-phosphate
-
-
-
-
?
ATP + 4-deoxypyridoxine
ADP + 4-deoxypyridoxine 5'-phosphate
-
-
-
-
?
ATP + 4-deoxypyridoxine
ADP + 4-deoxypyridoxine 5'-phosphate
-
-
-
-
?
ATP + 5-deoxypyridoxal
ADP + ?
-
-
-
-
?
ATP + 5-deoxypyridoxal
ADP + ?
-
-
-
-
?
ATP + 5-deoxypyridoxal
ADP + ?
-
-
-
-
?
ATP + 5-deoxypyridoxal
ADP + ?
-
-
-
-
?
ATP + 5-deoxypyridoxal
ADP + ?
-
-
-
-
?
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 + ginkgotoxin
?
-
ginkgotoxin is an effective pseudosubstrate
-
-
?
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 + omega-methylpyridoxal
ADP + omega-methylpyridoxal 5'-phosphate
-
-
-
-
?
ATP + pyridoxal
ADP + pyridoxal 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
-
-
-
-
ir
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
-
-
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
-
-
-
-
ir
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
-
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
-
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
-
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
-
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
-
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
-
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
-
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
-
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
-
-
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
-
-
-
?
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
-
-
?
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
-
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
-
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
-
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
-
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
-
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
-
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
-
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
-
-
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
-
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
-
-
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
-
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
-
-
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
-
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
-
-
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
-
-
-
ir
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
-
-
-
-
ir
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
no substrate: GTP
-
-
?
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
-
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
-
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
-
-
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
-
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
-
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
-
-
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
-
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
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
-
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
-
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
-
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
-
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
-
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
-
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
-
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
-
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
-
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
-
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
-
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
-
-
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
-
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
-
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
-
-
?
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
-
-
-
?
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
-
-
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
-
-
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
-
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
-
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
-
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
-
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
-
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
-
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
-
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
preferred substrate
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
-
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
-
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
-
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
-
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
-
-
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
-
important enzyme involved in bioactivation of vitamin B6
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
-
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 + pyridoxal
ADP + pyridoxal 5'-phosphate
-
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
-
-
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
-
-
-
?
ATP + pyridoxal
ADP + pyridoxal 5'-phosphate
-
-
-
?
ATP + pyridoxamine
ADP + pyridoxamine 5'-phosphate
-
-
-
-
ir
ATP + pyridoxamine
ADP + pyridoxamine 5'-phosphate
-
-
-
-
?
ATP + pyridoxamine
ADP + pyridoxamine 5'-phosphate
-
-
-
-
ir
ATP + pyridoxamine
ADP + pyridoxamine 5'-phosphate
-
-
-
-
?
ATP + pyridoxamine
ADP + pyridoxamine 5'-phosphate
-
-
-
-
?
ATP + pyridoxamine
ADP + pyridoxamine 5'-phosphate
-
-
-
?
ATP + pyridoxamine
ADP + pyridoxamine 5'-phosphate
-
-
-
-
?
ATP + pyridoxamine
ADP + pyridoxamine 5'-phosphate
-
-
-
?
ATP + pyridoxamine
ADP + pyridoxamine 5'-phosphate
-
-
-
ir
ATP + pyridoxamine
ADP + pyridoxamine 5'-phosphate
-
-
-
-
ir
ATP + pyridoxamine
ADP + pyridoxamine 5'-phosphate
-
-
-
?
ATP + pyridoxamine
ADP + pyridoxamine 5'-phosphate
-
-
-
?
ATP + pyridoxamine
ADP + pyridoxamine 5'-phosphate
-
-
-
-
?
ATP + pyridoxamine
ADP + pyridoxamine 5'-phosphate
-
-
-
?
ATP + pyridoxamine
ADP + pyridoxamine 5'-phosphate
-
33% of the activity with pyridoxal
-
-
?
ATP + pyridoxamine
ADP + pyridoxamine 5'-phosphate
-
-
-
-
?
ATP + pyridoxamine
ADP + pyridoxamine 5'-phosphate
-
-
-
?
ATP + pyridoxamine
ADP + pyridoxamine 5'-phosphate
-
not a substrate of the purified enzyme
-
-
?
ATP + pyridoxamine
ADP + pyridoxamine 5'-phosphate
-
study of substrate-enzyme interaction between immobilized pyridoxamine and recombinant porcine pyridoxal kinase using surface plasmon resonance biosensor
-
-
?
ATP + pyridoxamine
ADP + pyridoxamine 5'-phosphate
-
-
-
-
?
ATP + pyridoxine
ADP + pyridoxine 5'-phosphate
-
-
-
-
ir
ATP + pyridoxine
ADP + pyridoxine 5'-phosphate
-
-
-
-
?
ATP + pyridoxine
ADP + pyridoxine 5'-phosphate
-
-
-
-
ir
ATP + pyridoxine
ADP + pyridoxine 5'-phosphate
-
-
-
-
?
ATP + pyridoxine
ADP + pyridoxine 5'-phosphate
-
-
-
-
?
ATP + pyridoxine
ADP + pyridoxine 5'-phosphate
-
-
-
-
?
ATP + pyridoxine
ADP + pyridoxine 5'-phosphate
-
-
-
?
ATP + pyridoxine
ADP + pyridoxine 5'-phosphate
-
-
-
-
?
ATP + pyridoxine
ADP + pyridoxine 5'-phosphate
-
-
-
?
ATP + pyridoxine
ADP + pyridoxine 5'-phosphate
-
-
-
-
?
ATP + pyridoxine
ADP + pyridoxine 5'-phosphate
-
-
-
?
ATP + pyridoxine
ADP + pyridoxine 5'-phosphate
-
-
-
-
?
ATP + pyridoxine
ADP + pyridoxine 5'-phosphate
-
-
-
?
ATP + pyridoxine
ADP + pyridoxine 5'-phosphate
-
-
-
ir
ATP + pyridoxine
ADP + pyridoxine 5'-phosphate
-
-
-
-
?
ATP + pyridoxine
ADP + pyridoxine 5'-phosphate
-
-
-
?
ATP + pyridoxine
ADP + pyridoxine 5'-phosphate
-
-
-
?
ATP + pyridoxine
ADP + pyridoxine 5'-phosphate
-
-
-
-
?
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
-
-
-
?
ATP + pyridoxine
ADP + pyridoxine 5'-phosphate
-
-
-
-
?
ATP + pyridoxine
ADP + pyridoxine 5'-phosphate
-
-
-
-
?
ATP + pyridoxine
ADP + pyridoxine 5'-phosphate
-
-
-
?
ATP + pyridoxine
ADP + pyridoxine 5'-phosphate
-
-
-
?
ATP + pyridoxine
ADP + pyridoxine 5'-phosphate
-
46% of the activity with pyridoxal
-
-
?
ATP + pyridoxine
ADP + pyridoxine 5'-phosphate
-
-
-
-
?
pyridoxal + ATP
pyridoxal 5'-phosphate + ADP
-
-
-
?
pyridoxal + ATP
pyridoxal 5'-phosphate + ADP
-
-
-
-
?
additional information
?
-
-
the enzyme possesses also a 4-amino-5-hydroxymethyl-2-methylpyrimidine kinase activity
-
-
?
additional information
?
-
no activity with GTP
-
-
?
additional information
?
-
-
no activity with GTP
-
-
?
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
-
-
?
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Li+
-
poor activator which seems to modify the enzymatic mechanism from a random to an ordered sequential pattern with ATP bound before pyridoxal. Km: 37 mM
Rb+
-
Km: 5.3 mM. Monovalent cation required, activation in the order of decreasing efficiency: K+, Rb+, NH4+
Ca2+
-
Ca2+
-
divalent cation required, activation of the recombinant enzyme in the order of decreasing efficiency: Zn2+, Co2+, Mn2+, Mg2+, Ca2+
Co2+
-
Co2+
-
divalent cation required, activation of the recombinant enzyme in the order of decreasing efficiency: Zn2+, Co2+, Mn2+, Mg2+, Ca2+
Co2+
-
cations activate in decreasing order of efficiency: Co2+, Mn2+, Mg2+, Zn2+, Cu2+, Ni2+, Fe2+
Co2+
-
0.2 mM, partial activation
Cu2+
-
-
Cu2+
-
cations activate in decreasing order of efficiency: Co2+, Mn2+, Mg2+, Zn2+, Cu2+, Ni2+, Fe2+
Cu2+
-
0.2 mM, partial activation
Fe2+
-
Fe2+
-
cations activate in decreaseing order of efficiency: Co2+, Mn2+, Mg2+, Zn2+, Cu2+, Ni2+, Fe2+
K+
when only triethanolamine is present as the cation, K+ is an activator of the enzyme
K+
-
activates in presence of optimal concentrations of Zn2+
K+
in the absence of any potassium ion, the activity is less than 5% of the maximum activity
K+
-
most effective monovalent cation in activation. Improves both affinity for the substrates and maximal velocity. Km: 35 mM
K+
-
most effective activator of the monovalent cations
K+
affinity to pyridoxal and ATP is increased manifold in the presence of K+ compared to Na+, 2.5fold increase of activity
K+
activation. Affinity for ATP and pyridoxal is increased severalfold in presence of K+ compared with Na+, but the maximal activity of the Na+ form is more than double the activity of the K+ form
K+
-
Km: 8.9 mM. Monovalent cation required, activation in the order of decreasing efficiency: K+, Rb+, NH4+
Mg2+
-
-
Mg2+
-
active in the presence of Mg2+
Mg2+
-
in complex with ATP most likely preferred substrate in vivo
Mg2+
-
divalent cation required, activation of the recombinant enzyme in the order of decreasing efficiency: Zn2+, Co2+, Mn2+, Mg2+, Ca2+
Mg2+
-
cations activate in decreasing order of efficiency: Co2+, Mn2+, Mg2+, Zn2+, Cu2+, Ni2+, Fe2+
Mg2+
-
enzyme requires a divalent cation, optimal concentration is 0.416 mM
Mg2+
in complex with ATP most likely preferred substrate in vivo
Mg2+
acts in complex with ATP
Mg2+
required, bindings structure analysis, overview
Mg2+
required, Mg2+ ion can be located near the bound phosphate, it is coordinated with O3 of the ADP beta-phosphate and four water molecules
Mg2+
-
best activator, optimum activity at 0.25 mM Mn2+
Mn2+
-
Mn2+
-
divalent cation required, activation of the recombinant enzyme in the order of decreasing efficiency: Zn2+, Co2+, Mn2+, Mg2+, Ca2+
Mn2+
-
cations activate in decreasing order of efficiency: Co2+, Mn2+, Mg2+, Zn2+, Cu2+, Ni2+, Fe2+
Mn2+
-
0.2 mM, partial activation
Mn2+
-
0.2 mM, partial activation
Mn2+
-
0.2 mM, partial activation
Mn2+
-
optimum activity at 0.05 mM Mn2+
Na+
-
activates
Na+
-
increases maximal velocity and affinity for ATP, but decreases affinity for pyridoxal
Na+
6fold increase of activity
Na+
activation. Affinity for ATP and pyridoxal is increased severalfold in presence of K+ compared with Na+, but the maximal activity of the Na+ form is more than double the activity of the K+ form
Ni2+
-
-
Ni2+
-
cations activate in decreasing order of efficiency: Co2+, Mn2+, Mg2+, Zn2+, Cu2+, Ni2+, Fe2+
Ni2+
-
0.2 mM, partial activation
Zn2+
Zn2+ is the most effective cation for catalysis under saturating substrate concentrations
Zn2+
-
in complex with ATP preferred substrate in vitro
Zn2+
-
cations activate in decreasing order of efficiency: Co2+, Mn2+, Mg2+, Zn2+, Cu2+, Ni2+, Fe2+
Zn2+
-
divalent cation required, activation of the recombinant enzyme in the order of decreasing efficiency: Zn2+, Co2+, Mn2+, Mg2+, Ca2+. Optimum at about 0.1 mM Zn2+
Zn2+
-
divalent cation required, optimal concentration is 0.33 mM. Zn2+ is superior to Mg2+ below the optimum concentration of Zn2+
Zn2+
in complex with ATP preferred substrate in vitro
Zn2+
-
activator at low concentrations (0.019 mM optimal concentration), most effective divalent cation for catalysis
Zn2+
-
the enzyme requires divalent cations for activity. At 0.08 mM the cations activate in order of decreasing efficiency: Mn2+, Zn2+, Mg2+. At 0.4 mM the cations activate in the order of decreasing efficiency: Mn2+, Zn2+, Mg2+
Zn2+
-
half-maximal activation at 0.01 mM
additional information
the presence of 100 mM NaCl does not alter the potassium activation profile
additional information
-
the presence of 100 mM NaCl does not alter the potassium activation profile
additional information
Li+, Cs+, and Rb+ show no significant activity enhancement
additional information
-
Li+, Cs+, and Rb+ show no significant activity enhancement
additional information
no singnificant activity with Li+, Cs+, Rb+
additional information
-
no singnificant activity with Li+, Cs+, Rb+
additional information
the enzyme requires a metal cofactor, very low activity with Li+, Na+, K+, Rb+ and Cs+. Cobalt gives more activity when compared to that of Zn2+, Ca2+, Cu2+ and Ni2+. Cu2+ shows the least enzyme activity. Order of metal ions with increasing effect on enzyme activity is as follows: Co2+, Zn2+, Mn2+, Mg2+, Fe2+, Ca2+, Ni2+, Cu2+
additional information
-
the enzyme requires a metal cofactor, very low activity with Li+, Na+, K+, Rb+ and Cs+. Cobalt gives more activity when compared to that of Zn2+, Ca2+, Cu2+ and Ni2+. Cu2+ shows the least enzyme activity. Order of metal ions with increasing effect on enzyme activity is as follows: Co2+, Zn2+, Mn2+, Mg2+, Fe2+, Ca2+, Ni2+, Cu2+
additional information
-
ZnCl2 and Ca2+ do not activate the enzyme
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(2-Diethylaminoethyl)hydrazine
-
0.005 mM, 20% inhibition
1,1-Bis(2-diethylaminoethyl)hydrazine
-
0.005 mM, 51% inhibition
1,4-Diaminopiperazine
-
0.005 mM, 59% inhibition
1-(2-Hydrazinopropyl)piperidine
-
0.005 mM, 31% inhibition
1-(3-Dimethylamino-2-methylpropyl)hydrazine
-
0.005 mM, 39% inhibition
1-Aminopiperidine
-
0.005 mM, 58% inhibition
1-Cyclohexyl-1-methylhydrazine
-
0.005 mM, 29% inhibition
2,2'-hydrazinediethanol
-
0.005 mM, 47% inhibition
2,6-Dimethyl-3,4-bis(hydroxymethyl)pyridine
-
-
2-Methyl-3-amino-4,5,6-tris(hydroxymethyl)pyridine
-
-
2-Methyl-3-amino-4,5-bis(hydroxymethyl)pyridine
-
-
2-Methyl-3-hydroxy-5,6-bis(hydroxymethyl)pyridine
-
-
2-Methyl-4,5-bis(hydroxymethyl)pyridine
-
-
2-[1-(2-Diethylaminoethyl)hydrazine]ethanol
-
0.005 mM, 44% inhibition
3,4-dihydroxyphenylalanine
-
-
3-hydroxyanthranilic acid
-
IC50: 0.12 mM
3-hydroxykynurenine
-
IC50: 0.1 mM
4'-O-methylpyridoxine
i.e. ginkgotoxin. Treatment leads to temporarily reduced pyridoxal phosphate formation in vitro and possibly in vivo
4-Aminomorpholine
-
0.005 mM, 52% inhibition
5-dimethylaminonaphthalene-1-sulfonyl-4-aminobutyrate
-
competitive with respect to pyridoxal
5-hydroxytryptamine
-
0.5 mM, 11% inhibition of activity with pyridoxine, 81% inhibition of activity with pyridoxal
ADP
at high concentrations, product inhibition
alpha-Methylphenethylhydrazine
alpha-Methylphenethylhydrazone
aminooxyacetic acid
-
0.002 mM, 50% inhibition
Ca2+
-
low substrate inhibition
Caffeine
21% inhibition at 0.1 mM
Chloroquine
about 40% inhibition at 1 mM
cycloserine
-
0.1 mM, inhibits activity with pyridoxal, but not with pyridoxamine as substrate, 42% inhibition
D-penicillamine
-
0.1 mM, inhibits activity with pyridoxal, but not with pyridoxamine as substrate, 20% inhibition
enprofylline
33% inhibition at 0.1 mM
gamma-aminobutyric acid
-
-
isoniazid
-
0.1 mM, inhibits activity with pyridoxal, but not with pyridoxamine as substrate, 81% inhibition
K+
-
at high concentrations
L-canaline
-
0.01 mM, 50% inhibition
lamotrigine
45% inhibition at 0.1 mM
levodopa
-
0.1 mM, inhibits activity with pyridoxal, but not with pyridoxamine as substrate, 16% inhibition
Li+
-
at high concentrations
Mn2+
-
excess free divalent cations inhibit the enzyme
muzolimine
-
0.1 mM, inhibits activity with pyridoxal, but not with pyridoxamine as substrate, 27% inhibition
N,N'-Bis(pyridoxyl)hydrazine
-
0.0005 mM, 50% inhibition
N-Dansyl-1,8-diaminooctane
NADH
-
0.5 mM, 14% inhibition of activity with pyridoxine, 11% inhibition of activity with pyridoxal
Octylhydrazine
-
0.005 mM, 53% inhibition
picolinate
-
0.5 mM, 95% inhibition of activity with pyridoxine, 97% inhibition of activity with pyridoxal
progabide
-
0.1 mM, inhibits using either pyridoxamine or pyridoxal as substrate
pyridoxal semicarbazone
-
0.00005 mM, 50% inhibition
pyridoxal-gamma-aminobutyrate
-
-
pyridoxine
-
substrate inhibition above 0.2 mM
quinolinate
-
0.5 mM, 82% inhibition of activity with pyridoxine, 82% inhibition of activity with pyridoxal
quinolinic acid
-
IC50: 0.42 mM
rugulactone
selectively modifies the enzyme not at the active site cysteine, but on a remote cysteine residue
Semicarbazine
-
0.0005 mM, 50% inhibition
Theobromine
22% inhibition at 0.1 mM
Thiamphenicol
-
0.1 mM, inhibits activity with pyridoxal, but not with pyridoxamine as substrate, 31% inhibition
xanthurenate
-
0.5 mM, 19% inhibition of activity with pyridoxine, 18% inhibition of activity with pyridoxal
xanthurenic acid
-
IC50: 0.36 mM
ZnATP2-
-
weak substrate inhibition
(R)-roscovitine
-
-
(R)-roscovitine
binds to the pyridoxal binding site
4-deoxypyridoxine
-
-
4-deoxypyridoxine
-
competitive with respect to pyridoxal
alpha-Methylphenethylhydrazine
-
0.001 mM, 50% inhibition
alpha-Methylphenethylhydrazine
-
0.015 mM, 50% inhibition
alpha-Methylphenethylhydrazone
-
0.001 mM, 50% inhibition
alpha-Methylphenethylhydrazone
-
0.015 mM, 50% inhibition
azine
-
0.000065 mM, 50% inhibition
azine
-
0.0004 mM, 50% inhibition
dopamine
-
-
dopamine
-
0.1 mM, inhibits activity with pyridoxal, but not with pyridoxamine as substrate, 52% inhibition
ginkgotoxin
-
ginkgotoxin
i.e. 4'-O-methylpyridoxine, complete inhibition at 0.1 mM
ginkgotoxin
-
i.e.4'-O-methylpyridoxine
hydrazine
-
0.00055 mM, 50% inhibition
hydrazine
-
0.05 mM, 50% inhibition
hydroxylamine
-
0.0005 mM, 50% inhibition
hydroxylamine
-
0.01 mM, 50% inhibition
Mg2+
-
excess free divalent cations inhibit the enzyme
Mg2+
-
low substrate inhibition
N-Dansyl-1,8-diaminooctane
-
-
N-Dansyl-1,8-diaminooctane
-
-
Na+
-
at high concentrations
Oxime
-
0.0025 mM, 50% inhibition
Oxime
-
0.008 mM, 50% inhibition
primaquine
-
competitive inhibition, complete inhibition at 0.75 mM
primaquine
competitive inhibition, complete inhibition at 1 mM
primaquine
competitive inhibition, about 70% inhibition at 1 mM
pyridoxal
-
-
pyridoxal
-
effective competitive inhibitor
pyridoxal
-
substrate inhibition
pyridoxal
at high concentrations, substrate inhibition
pyridoxal
-
0.1 mM, substrate inhibition
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
at high concentrations, product inhibition
pyridoxaloxime
-
strong competitive inhibitor
pyridoxaloxime
-
competitive with respect to pyridoxal
pyridoxamine
-
effective competitive inhibitor
serotonin
-
-
serotonin
-
0.08 mM, 50% inhibition
theophylline
-
0.1 mM, inhibits using either pyridoxamine or pyridoxal as substrate, 86% inhibition of reaction with pyridoxal, 88% inhibition of reaction with pyridoxamine
theophylline
60% inhibition at 0.1 mM
tryptamine
-
no inhibition of activity with pyridoxine, 72% inhibition of activity with pyridoxal
Zn2+
-
slight inhibition above the optimum of 0.33 mM
Zn2+
-
excess free divalent cations inhibit the enzyme
Zn2+
-
ZnCl2 shows pronounced high substrate inhibition
additional information
-
no inhibition by Tyr, Trp and 5-hydroxytryptophan
-
additional information
-
ATP4- and HATP3- do not affect the enzyme activity. Free Mg2+ does not inhibit enzyme activity
-
additional information
-
not inhibited by chloroquine
-
additional information
not inhibited by chloroquine
-
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0.0216
4'-deoxypyridoxine
0.00495
4'-O-methylpyridoxine
pH 6.2, 37°C
1.85 - 2.03
4-Amino-5-hydroxymethyl-2-methylpyrimidine
0.00495 - 0.0466
ginkgotoxin
0.00122 - 3.839
pyridoxal
0.006 - 0.1818
pyridoxamine
0.00172 - 2.07
pyridoxine
additional information
additional information
-
0.0216
4'-deoxypyridoxine
pH 6.2, 37°C
0.0216
4'-deoxypyridoxine
in 70 mM potassium phosphate buffer, pH 6.2
1.85
4-Amino-5-hydroxymethyl-2-methylpyrimidine
mutant C110A, pH not specified in the publication, temperature not specified in the publication
1.99
4-Amino-5-hydroxymethyl-2-methylpyrimidine
wild-type, pH not specified in the publication, temperature not specified in the publication
2.03
4-Amino-5-hydroxymethyl-2-methylpyrimidine
-
pH 8, 37°C
0.0091
ATP
-
pH 7, 37°C
0.02
ATP
-
in the presence of Zn2+, at pH 6.5 and 37°C
0.025
ATP
in the presence of K+, and in complex with Mg2+
0.025
ATP
presence of 40 mM Na+, pH 7.3, 37°C
0.0579
ATP
in 70 mM potassium phosphate (pH 5.5), 0.5 mM ZnCl2, at 37°C
0.06
ATP
-
ATP in form of ZnATP2-
0.07
ATP
-
kinase 1 with pyridoxal as substrate, pH 7.3, 37°C
0.07
ATP
-
ATP in form of ZnATP2-
0.078
ATP
-
mutant enzyme C124A, at pH 7.4 and 37°C
0.1
ATP
with pyridoxal, pH 6.6, 37°C
0.101
ATP
-
ATP in form of MgATP2-
0.102
ATP
-
wild type enzyme, at pH 7.4 and 37°C
0.12
ATP
with pyridoxamine, pH 8.5, 37°C
0.127
ATP
-
pH 7, 37°C, recombinant enzyme
0.17
ATP
D235A mutant protein
0.17
ATP
ATP in form of MgATP
0.18
ATP
D235N mutant protein
0.18
ATP
ATP in form of MgATP
0.19
ATP
wild-type protein
0.19
ATP
ATP in form of MgATP
0.194
ATP
-
ATP in form of MnATP2-
0.2
ATP
recombinant wild-type enzyme, pH 7.2, 37°C
0.377
ATP
pH 7.3, 37°C recombinant mutant D87H
0.407
ATP
pH 7.3, 37°C recombinant wild-type enzyme
0.42
ATP
with pyridoxal as substrate, pH 7.3, 37°C
0.42
ATP
ATP in form of MgATP
0.5
ATP
in the presence of Na+, and in complex with Mg2+
0.5
ATP
presence of 40 mM Na+, pH 7.3, 37°C
0.6
ATP
-
kinase 1 with pyridoxal as substrate, pH 7.3, 37°C
0.6
ATP
-
ATP in form of MgATP2-
0.901
ATP
pH 7.3, 37°C recombinant mutant H246Q
1.024
ATP
pH 7.3, 37°C recombinant mutant A243G
3.096
ATP
pH 7.3, 37°C recombinant mutant V128I
0.00495
ginkgotoxin
in 70 mM potassium phosphate buffer, pH 6.2
0.0297
ginkgotoxin
recombinant enzyme, pH 7.5, 37°C
0.0466
ginkgotoxin
-
recombinant enzyme, apparent value, in HEPES/MgCl2 pH 7.4, 0.15 mM ZnCl2, at 37°C
0.00122
pyridoxal
-
in the presence of K+, at pH 7.0 and 30°C
0.00165
pyridoxal
-
recombinant enzyme, apparent value, in HEPES/MgCl2 pH 7.4, 0.15 mM ZnCl2, at 37°C
0.0028
pyridoxal
in 70 mM potassium phosphate buffer, pH 6.2
0.01
pyridoxal
in the presence of K+
0.01
pyridoxal
presence of 40 mM Na+, pH 7.3, 37°C
0.0153
pyridoxal
in the presence of K+, at pH 7.0 and 30°C
0.0216
pyridoxal
in the presence of K+, at pH 7.0 and 30°C
0.022
pyridoxal
-
pH 7, 37°C
0.024
pyridoxal
wild-type protein
0.025
pyridoxal
-
pH 6, 37°C
0.03
pyridoxal
with MgATP2- as substrate, pH 7.3, 37°C
0.037
pyridoxal
-
mutant enzyme C124A, at pH 7.4 and 37°C
0.038
pyridoxal
-
pH 7, 37°C, recombinant enzyme
0.038
pyridoxal
-
recombinant enzyme, apparent value, in 70 mM potassium phosphate pH 7.0, 0.15 mM ZnCl2, at 37°C
0.044
pyridoxal
pH 6.6, 37°C
0.0441
pyridoxal
in 70 mM potassium phosphate (pH 5.5), 0.5 mM ZnCl2, at 37°C
0.047
pyridoxal
-
pH 8, 37°C
0.053
pyridoxal
-
wild type enzyme, at pH 7.4 and 37°C
0.058
pyridoxal
D235N mutant protein
0.0587
pyridoxal
pH 6.2, 37°C
0.07
pyridoxal
-
pH 6.5, 30°C
0.0739
pyridoxal
-
in the presence of Na+, at pH 7.0 and 30°C
0.075
pyridoxal
in the presence of Na+
0.075
pyridoxal
presence of 40 mM Na+, pH 7.3, 37°C
0.0909
pyridoxal
recombinant enzyme, pH 7.5, 37°C
0.097
pyridoxal
-
pH 7, 37°C
0.1
pyridoxal
-
kinase 1 with MgATP2- as substrate, pH 7.3, 37°C
0.111
pyridoxal
wild-type, pH not specified in the publication, temperature not specified in the publication
0.141
pyridoxal
pH 7.3, 37°C recombinant mutant H246Q
0.17
pyridoxal
D235A mutant protein
0.177
pyridoxal
pH 7.3, 37°C recombinant mutant A243G
0.189
pyridoxal
pH 7.3, 37°C recombinant wild-type enzyme
0.19
pyridoxal
-
kinase 1 with ZnATP2- as substrate, pH 7.3, 37°C
0.24
pyridoxal
recombinant wild-type enzyme, pH 7.2, 37°C
0.26
pyridoxal
mutant C214D, pH not specified in the publication, temperature not specified in the publication
0.35
pyridoxal
with ZnATP2- as substrate, pH 7.3, 37°C
0.49
pyridoxal
-
at pH 6.5 and 37°C
2.09
pyridoxal
pH 7.3, 37°C recombinant mutant D87H
3.839
pyridoxal
pH 7.3, 37°C recombinant mutant V128I
0.006
pyridoxamine
-
pH 6.5
0.01
pyridoxamine
-
kinase 1 with ZnATP2- as substrate, pH 7.3, 37°C
0.03
pyridoxamine
-
kinase 1 with MgATP2- as substrate, pH 7.3, 37°C
0.035
pyridoxamine
with MgATP2- as substrate, pH 7.3, 37°C
0.0594
pyridoxamine
-
recombinant enzyme, apparent value, in HEPES/MgCl2 pH 7.4, 0.15 mM ZnCl2, at 37°C
0.06
pyridoxamine
pH 8.5, 37°C
0.126
pyridoxamine
pH 6.2, 37°C
0.126
pyridoxamine
in 70 mM potassium phosphate buffer, pH 6.2
0.1818
pyridoxamine
recombinant enzyme, pH 7.5, 37°C
0.00172
pyridoxine
-
pH 7.0, 37°C
0.00987
pyridoxine
pH 6.2, 37°C
0.00987
pyridoxine
in 70 mM potassium phosphate buffer, pH 6.2
0.015
pyridoxine
with ZnATP2- as substrate, pH 7.3, 37°C
0.017
pyridoxine
-
pH 6.0, 37°C
0.02
pyridoxine
with MgATP2- as substrate, pH 7.3, 37°C
0.025
pyridoxine
-
kinase 1 with MgATP2- as substrate, pH 7.3, 37°C
0.026
pyridoxine
-
pH 6.5
0.048
pyridoxine
-
recombinant enzyme, apparent value, in HEPES/MgCl2 pH 7.4, 0.15 mM ZnCl2, at 37°C
0.06
pyridoxine
-
pH 5.8, 37°C, with MnATP2- as the second substrate
0.212
pyridoxine
-
pH 6.5, 30°C
0.4347
pyridoxine
recombinant enzyme, pH 7.5, 37°C
1.51
pyridoxine
mutant C110A, pH not specified in the publication, temperature not specified in the publication
2.07
pyridoxine
wild-type, pH not specified in the publication, temperature not specified in the publication
additional information
additional information
steady-state kinetics
-
additional information
additional information
-
effect of KCl on Km-values
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
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evolution
PdxK belongs to ribokinase enzyme family in which either cysteine or aspartate act as catalytic residue for its activity. The known catalytic mechanism of ribokinase family and for PdxK is the in line displacement mechanism in which hydroxyl group of the substrate is activated by a catalytic base (aspartate) of the enzyme, to make the nucleophilic attack on the gamma-phosphate group of ATP. The active site residues Leu43, Ser47, Ile52, Arg56, Asn87 and Thr227 present in LdPdxK are replaced with Phe43, Thr47, Try52, Val56, Arg86 and Val231 in mammalian PdxKs
evolution
pyridoxine/pyridoxal kinase (PdxK) belongs to the ribokinase family and is involved in the vitamin B6 salvage pathway by phosphorylating pyridoxal (PL) into an active form. In the human malaria parasite, Plasmodium falciparum, PfPdxK functions to salvage vitamin B6 from both itself and its host
evolution
-
PdxK belongs to ribokinase enzyme family in which either cysteine or aspartate act as catalytic residue for its activity. The known catalytic mechanism of ribokinase family and for PdxK is the in line displacement mechanism in which hydroxyl group of the substrate is activated by a catalytic base (aspartate) of the enzyme, to make the nucleophilic attack on the gamma-phosphate group of ATP. The active site residues Leu43, Ser47, Ile52, Arg56, Asn87 and Thr227 present in LdPdxK are replaced with Phe43, Thr47, Try52, Val56, Arg86 and Val231 in mammalian PdxKs
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malfunction
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root growth of a sos4 mutant is significantly decreased when grown on either 100 mM or 200 mM sucrose as compared to root growth on10 mM sucrose. The sos4 mutant plant accumulates phytoglycogen
malfunction
in Drosophila, mutations in the dPdxk gene cause chromosome aberrations (CABs) and increased glucose content in larval hemolymph. The phenotype is rescued by the expression of wild-type human PDXK enzyme, although not by human PDXK mutants D87H, V128I, H246Q, and A243G
malfunction
the four PDXK human variants, D87H, V128I, H246Q, and A243Gf D87H, V128I, H246Q and A243G proteins show reduced catalytic activity and/or reduced affinity for PLP precursors. Although these variants are rare in population and carried in heterozygous condition, it is suggested that in certain metabolic contexts and diseases in which PLP levels are reduced, the presence of these PDXK variants might threaten genome integrity and increase cancer risk
physiological function
pyridoxal kinase is a key enzyme in the metabolism of vitamin B6
physiological function
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the enzyme is essential for growth of Trypanosoma brucei in vitro and for infectivity in mice
physiological function
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the SOS4 pyridoxal kinase is required for maintenance of vitamin B6-mediated processes in chloroplasts. SOS4 is required for maintenance of phosphorylated B6 vitamer concentrations in chloroplasts
physiological function
biotransformation of pyridoxal to pyridoxal 5'-phosphate (PLP) by pyridoxal kinase (pdxY) supports cadaverine production in Escherichia coli. PLP is an essential cofactor of lysine decarboxylase and the major bottleneck in the cadaverine biosynthesis pathway
physiological function
in eukaryotes, pyridoxal kinase (PDXK) acts in vitamin B6 salvage pathway to produce pyridoxal 5'-phosphate (PLP), the active form of the vitamin, which is implicated in numerous crucial metabolic reactions. PDXK converts PLP precursors such as pyridoxal (PL), pyridoxamine (PM) and pyridoxine (PN) taken from food into PLP, PMP and PNP, respectively. PNPO catalyzes the oxidation of PMP and PNP into PLP. PLP performs many functions by working as coenzyme for a wide number of enzymes which control amino acid, lipid and carbohydrate metabolism
physiological function
in eukaryotes, pyridoxal kinase (PDXK) acts in vitamin B6 salvage pathway to produce pyridoxal 5'-phosphate (PLP), the active form of the vitamin, which is implicated in numerous crucial metabolic reactions. PDXK converts PLP precursors such as pyridoxal (PL), pyridoxamine (PM) and pyridoxine (PN) taken from food into PLP, PMP and PNP, respectively. PNPO catalyzes the oxidation of PMP and PNP into PLP. PLP performs many functions by working as coenzyme for a wide number of enzymes which control amino acid, lipid and carbohydrate metabolism
physiological function
pyridoxal kinase (PdxK) is an important enzyme of the vitamin B6 salvage pathway which is required for phosphorylation of B6 vitamers
physiological function
pyridoxine/pyridoxal kinase (PdxK) belongs to the ribokinase family and is involved in the vitamin B6 salvage pathway by phosphorylating pyridoxal (PL) into an active form. In the human malaria parasite, Plasmodium falciparum, PfPdxK functions to salvage vitamin B6 from both itself and its host
physiological function
the enzyme pyridoxal kinase (PdxK) catalyzes the conversion of pyridoxal to pyridoxal 5'-phosphate (PLP) using ATP as the cosubstrate. The product PLP plays a key role in several biological processes such as transamination, decarboxylation and deamination
physiological function
vitamin B6 enters the cells after hydrolysis of the phosphorylated forms by the membrane-bound tissue non-specific alkaline phosphatase (TNSALP, EC 3.1.3.1). Once inside the cells, pyridoxal kinase (PL kinase, PDXK, EC 2.7.1.35) phosphorylates the hydroxymethyl group of PL, PN and PM to their respective 5'-phosphate forms
physiological function
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pyridoxal kinase (PdxK) is an important enzyme of the vitamin B6 salvage pathway which is required for phosphorylation of B6 vitamers
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physiological function
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the enzyme pyridoxal kinase (PdxK) catalyzes the conversion of pyridoxal to pyridoxal 5'-phosphate (PLP) using ATP as the cosubstrate. The product PLP plays a key role in several biological processes such as transamination, decarboxylation and deamination
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additional information
experimental resurrection of the last common ancestor of the hydroxymethyl pyrimidine kinase group based on comparison of hydroxymethyl pyrimidine and pyridoxal kinases. Probably the last common ancestor was not able to use pyridoxal under physiological conditions. The pyridoxal kinase activity present in the current bifunctional enzymes must have appeared in a convergent event independently of the pyridoxal kinase activity of pdxY and pdxK genes. Substrate pyridoxal is 8-times less preferred than the phosphorylation of hydroxymethyl pyrimidine by the last ancestor
additional information
a FIxxIIxL motif at the C-terminus of the disordered repeat motif (XNXH)m that is implicated in binding the WD40 domain and may provide temporal control of PfPdxK through an interaction with a E3 ligase complex. Molecular docking and modelling, overview. Binding structure of AMP-PNP with PdxK
additional information
analysis of the binding structures of substrates and products from PdxK-ligand crystal structures, overview
additional information
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analysis of the binding structures of substrates and products from PdxK-ligand crystal structures, overview
additional information
comparison of the structure of apo StPLK with its ligand-bound forms
additional information
in silico analysis of the human and parasite PdxK structure revealing significant differences in the active site region, LdPdxK homology modeling using pyridoxal kinase from Trypanosoma brucei (PDB ID 3ZS7) as a template, molecular dynamics and molecular docking, overview
additional information
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in silico analysis of the human and parasite PdxK structure revealing significant differences in the active site region, LdPdxK homology modeling using pyridoxal kinase from Trypanosoma brucei (PDB ID 3ZS7) as a template, molecular dynamics and molecular docking, overview
additional information
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in silico analysis of the human and parasite PdxK structure revealing significant differences in the active site region, LdPdxK homology modeling using pyridoxal kinase from Trypanosoma brucei (PDB ID 3ZS7) as a template, molecular dynamics and molecular docking, overview
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additional information
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analysis of the binding structures of substrates and products from PdxK-ligand crystal structures, overview
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Kumar, V.; Sharma, M.; Rakesh, B.R.; Malik, C.K.; Neelagiri, S.; Neerupudi, K.B.; Garg, P.; Singh, S.
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Leishmania donovani (A0A0G2YFI9), Leishmania donovani, Leishmania donovani MHOM/80/IN/Dd8 (A0A0G2YFI9)
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Are, S.; Gatreddi, S.; Jakkula, P.; Qureshi, I.A.
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Leishmania donovani (A0A0G2YFI9), Leishmania donovani, Leishmania donovani MHOM/80/IN/Dd8 (A0A0G2YFI9)
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