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Literature summary for 2.7.1.35 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
Search for more literature for 2.7.1.35

Cloned(Commentary)

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

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging drop vapour diffusion method using 100 mM Tris-HCl pH 8.0 and 50% 2-methyl-2,4-pentanediol Homo sapiens
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

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

KM Value [mM]

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

Metals/Ions

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

Organism UniProt Comment Textmining
Homo sapiens O00764
-
-

Purification (Commentary)

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

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
dimer x-ray crystallography Homo sapiens

Synonyms

Synonyms Comment Organism
PLK
-
 Homo sapiens

Turnover Number [1/s]

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

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Homo sapiens