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Literature summary extracted from

  • Musayev, F.N.; Di Salvo, M.L.; Ko, T.P.; Gandhi, A.K.; Goswami, A.; Schirch, V.; Safo, M.K.
    Crystal Structure of human pyridoxal kinase: Structural basis of M+ and M2+ activation (2007), Protein Sci., 16, 2184-2194.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.1.35 expressed in Escherichia coli Rosetta (DE3)pLysS cells Homo sapiens
2.7.1.35 expression in Escherichia coli Homo sapiens

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.7.1.35 hanging drop vapour diffusion method using 100 mM Tris-HCl pH 8.0 and 50% 2-methyl-2,4-pentanediol Homo sapiens
2.7.1.35 unliganded enzyme and in complex with MgATP, diffraction to 2.0 and 2.2 A rsolution, respectively. both Structures show similar open conformations. Mg2+ and Na+ act in tandem to anchor the ATP at the active site, which itself acts as a sink to bind several molecules of 2-methyl-2,4-pentanediol Homo sapiens

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.1.35 Na+ inhibits above 50 mM Homo sapiens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.1.35 0.01
-
 pyridoxal in the presence of K+ Homo sapiens
2.7.1.35 0.01
-
 pyridoxal presence of 40 mM Na+, pH 7.3, 37°C Homo sapiens
2.7.1.35 0.025
-
 ATP in the presence of K+, and in complex with Mg2+ Homo sapiens
2.7.1.35 0.025
-
 ATP presence of 40 mM Na+, pH 7.3, 37°C Homo sapiens
2.7.1.35 0.075
-
 pyridoxal in the presence of Na+ Homo sapiens
2.7.1.35 0.075
-
 pyridoxal presence of 40 mM Na+, pH 7.3, 37°C Homo sapiens
2.7.1.35 0.5
-
 ATP in the presence of Na+, and in complex with Mg2+ Homo sapiens
2.7.1.35 0.5
-
 ATP presence of 40 mM Na+, pH 7.3, 37°C Homo sapiens

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.1.35 K+ affinity to pyridoxal and ATP is increased manifold in the presence of K+ compared to Na+, 2.5fold increase of activity Homo sapiens
2.7.1.35 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 Homo sapiens
2.7.1.35 Mg2+ acts in complex with ATP Homo sapiens
2.7.1.35 additional information Li+, Cs+, and Rb+ show no significant activity enhancement Homo sapiens
2.7.1.35 additional information no singnificant activity with Li+, Cs+, Rb+ Homo sapiens
2.7.1.35 Na+ 6fold increase of activity Homo sapiens
2.7.1.35 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 Homo sapiens

Organism

EC Number Organism UniProt Comment Textmining
2.7.1.35 Homo sapiens O00764
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.1.35 TMAE column chromatography, Phenyl Sepharose column chromatography, and hydroxyapatite column chromatography Homo sapiens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.1.35 ATP + pyridoxal
-
 Homo sapiens ADP + pyridoxal 5'-phosphate
-
 ?
2.7.1.35 ATP + pyridoxamine
-
 Homo sapiens ADP + pyridoxamine 5'-phosphate
-
 ?
2.7.1.35 ATP + pyridoxine
-
 Homo sapiens ADP + pyridoxine 5'-phosphate
-
 ?

Subunits

EC Number Subunits Comment Organism
2.7.1.35 dimer x-ray crystallography Homo sapiens

Synonyms

EC Number Synonyms Comment Organism
2.7.1.35 PLK
-
 Homo sapiens

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.7.1.35 1.42
-
 pyridoxal presence of 40 mM K+, pH 7.3, 37°C Homo sapiens
2.7.1.35 3.3
-
 pyridoxal presence of 40 mM Na+, pH 7.3, 37°C Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
2.7.1.35 ATP
-
 Homo sapiens