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Information on EC 2.7.1.35 - pyridoxal kinase and Organism(s) Ovis aries and UniProt Accession P82197
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2.7.1.35 pyridoxal kinaseIUBMB Comments
Pyridoxine, pyridoxamine and various derivatives can also act as acceptors.
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Word Map
- 2.7.1.35
- 5'-phosphate
-
vitamers
- pyridoxal-5'-phosphate
-
plp-dependent
-
4-pyridoxic
- ribokinase
- agriculture
- synthesis
- drug development
- medicine
The taxonomic range for the selected organisms is: Ovis aries
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
pyridoxal kinase, pyridoxine kinase, pl kinase, ldpdxk, pyridoxal phosphokinase, stplk, pn kinase, hpl kinase, epl kinase 1, salt overly sensitive4, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
kinase (phosphorylating), pyridoxal
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kinase, pyridoxal (phosphorylating)
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PL kinase
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PLK
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PM kinase
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PN kinase
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-
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PN/PL/PM kinase
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-
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pyridoxal 5-phosphate-kinase
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-
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pyridoxal kinase
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-
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pyridoxal kinase-like protein SOS4
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pyridoxal phosphokinase
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pyridoxamine kinase
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pyridoxine kinase
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pyridoxine/pyridoxal/pyridoxamine kinase
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vitamin B6 kinase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phospho group transfer
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-
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SYSTEMATIC NAME
IUBMB Comments
ATP:pyridoxal 5'-phosphotransferase
Pyridoxine, pyridoxamine and various derivatives can also act as acceptors.
CAS REGISTRY NUMBER
COMMENTARY
9026-42-0
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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 + 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
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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 + pyridoxamine
ADP + pyridoxamine 5'-phosphate
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33% of the activity with pyridoxal
-
-
?
ATP + pyridoxine
ADP + pyridoxine 5'-phosphate
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40% of the activity with pyridoxal
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-
?
NATURAL SUBSTRATE
NATURAL 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 + 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
-
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
-
generates the active form of vitamin B6, which serves as cofactor for many enzymes
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-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K+
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Km: 8.9 mM. Monovalent cation required, activation in the order of decreasing efficiency: K+, Rb+, NH4+
Rb+
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Km: 5.3 mM. Monovalent cation required, activation in the order of decreasing efficiency: K+, Rb+, NH4+
Zn2+
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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+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NH4+
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Km: 3.7 mM. Monovalent cation required, activation in the order of decreasing efficiency: K+, Rb+, NH4+
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PDXK_SHEEP
312
0
34819
Swiss-Prot
other Location (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, in complex with (R)-roscovitine and N6-methyl-(R)-roscovitine
crystallized in the orthorhombic form using the hanging-drop vapour-diffusion method with sodium citrate as the precipitant, crystals are transferred into a soaking liquid without citrate and two-heavy-atom derivatives are prepared
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crystals are grown in the presence of 100 mM potassium phosphate, pH 7.2, and 120 mM ammonium sulfate and crystals grown in the presence of 600 mM potassium phosphate, pH 7.2, and in the absence of ammonium sulfate. The crystals are quite stable to X-rays and diffract at 2.2 A resolution
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hanging drop vapor diffusion method in complex with adenosine 5-(beta, gamma-methylenetriphosphate)-pyridoxamine, ADP-pyriodoxal 5-phosphate, and ADP
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the enzyme is digested by chymotrypsin to proteolytic fragments of 24000 Da and 16000 Da
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Arone, A.; Rogers, P.; Scholz, G.; Kwok, F.
Crystallization and preliminary X-ray studies of pyridoxal kinase from sheep brain
J. Biol. Chem.
264
4322-4323
1989
Ovis aries
Karawya, E.; Mostafa, M.H.; Osman, N.
The kinetic mechanism of inhibition of liver pyridoxal kinase with tryptophan metabolites
Biochim. Biophys. Acta
657
153-158
1981
Ovis aries
Kwok, F.; Kerry, J.A.; Churchich, J.E.
Sheep brain pyridoxal kinase: fluorescence spectroscopy of the dimeric enzyme
Biochim. Biophys. Acta
874
167-173
1986
Ovis aries
Kerry, J.A.; Rohde, M.; Kwok, F.
Brain pyridoxal kinase. Purification and characterization
Eur. J. Biochem.
158
581-585
1986
Ovis aries
Karawya, E.; Fonda, M.L.
Physical and kinetic properties of sheep liver pyridoxine kinase
Arch. Biochem. Biophys.
216
170-177
1982
Ovis aries
Li, M.H.; Kwok, F.; An, X.M.; Chang, W.R.; Lau, C.K.; Zhang, J.P.; Liu, S.Q.; Leung, Y.C.; Jiang, T.; Liang, D.C.
Crystallization and preliminary crystallographic studies of pyridoxal kinase from sheep brain
Acta Crystallogr. Sect. D
58
1479-1481
2002
Ovis aries
Maras, B.; Valiante, S.; Orru, S.; Simmaco, M.; Barra, D.; Churchich, J.E.
Structure of pyridoxal kinase from sheep brain and role of the tryptophanyl residues
J. Protein Chem.
18
259-268
1999
Ovis aries
Cho, J.J.; Kim, S.K.; Kim, Y.T.
Catalytic and structural properties of pyridoxal kinase
J. Biochem. Mol. Biol.
30
125-131
1997
Ovis aries
-
Li, M.H.; Kwok, F.; Chang, W.R.; Liu, S.Q.; Lo, S.C.; Zhang, J.P.; Jiang, T.; Liang, D.C.
Conformational changes in the reaction of pyridoxal kinase
J. Biol. Chem.
279
17459-17465
2004
Ovis aries
Tang, L.; Li, M.H.; Cao, P.; Wang, F.; Chang, W.R.; Bach, S.; Reinhardt, J.; Ferandin, Y.; Galons, H.; Wan, Y.; Gray, N.; Meijer, L.; Jiang, T.; Liang, D.C.
Crystal structure of pyridoxal kinase in complex with roscovitine and derivatives
J. Biol. Chem.
280
31220-31229
2005
Ovis aries (P82197)
Bach, S.; Knockaert, M.; Reinhardt, J.; Lozach, O.; Schmitt, S.; Baratte, B.; Koken, M.; Coburn, S.P.; Tang, L.; Jiang, T.; Liang, D.C.; Galons, H.; Dierick, J.F.; Pinna, L.A.; Meggio, F.; Totzke, F.; Schaechtele, C.; Lerman, A.S.; Carnero, A.; Wan, Y.; Gray, N.; Meijer, L.
Roscovitine targets, protein kinases and pyridoxal kinase
J. Biol. Chem.
280
31208-31219
2005
Ovis aries, Homo sapiens
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