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Literature summary extracted from

  • Lee, H.S.; Moon, B.J.; Choi, S.Y.; Kwon, O.S.
    Human pyridoxal kinase: overexpression and properties of the recombinant enzyme (2000), Mol. Cells, 10, 452-459.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.1.35 recombinant enzyme is overexpressed in Escherichia coli as a fusion protein with maltose binding protein Homo sapiens

General Stability

EC Number General Stability Organism
2.7.1.35 3 M guanidine hydrochloride, enzyme loses more than 90% of the alpha-helix content Homo sapiens

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.1.35 Cr2+
-
 Homo sapiens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.1.35 0.012
-
 ATP pH 7, 37°C Homo sapiens
2.7.1.35 0.097
-
 pyridoxal pH 7, 37°C Homo sapiens

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.1.35 Ca2+ divalent cation required, activation of the recombinant enzyme in the order of decreasing efficiency: Zn2+, Co2+, Mn2+, Mg2+, Ca2+ Homo sapiens
2.7.1.35 Co2+ divalent cation required, activation of the recombinant enzyme in the order of decreasing efficiency: Zn2+, Co2+, Mn2+, Mg2+, Ca2+ Homo sapiens
2.7.1.35 Mg2+ divalent cation required, activation of the recombinant enzyme in the order of decreasing efficiency: Zn2+, Co2+, Mn2+, Mg2+, Ca2+ Homo sapiens
2.7.1.35 Mn2+ divalent cation required, activation of the recombinant enzyme in the order of decreasing efficiency: Zn2+, Co2+, Mn2+, Mg2+, Ca2+ Homo sapiens
2.7.1.35 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+ Homo sapiens

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.7.1.35 40000
-
 gel filtration Homo sapiens

Organism

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

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.1.35 recombinant enzyme Homo sapiens

Renatured (Commentary)

EC Number Renatured (Comment) Organism
2.7.1.35 the enzyme which has lost more than 90% of the alpha-helix content after treatment with 3 M guanidine hydrochloride regains more than 90% of the original catalytic activity after overnight dialysis against 10 mM potassium phosphate, pH 7 at 4°C Homo sapiens

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.7.1.35 2.47
-
-
 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
-
 ?

Subunits

EC Number Subunits Comment Organism
2.7.1.35 monomer 1 * 40000, SDS-PAGE Homo sapiens

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
2.7.1.35 25
-
 pH 5.5-11, 3 h, stable Homo sapiens

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.7.1.35 5.5 6
-
 Homo sapiens

pH Range

EC Number pH Minimum pH Maximum Comment Organism
2.7.1.35 5 8 pH 5.0: about 70% of maximal activity, pH 8.0: about 50% of maximal activity Homo sapiens

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
2.7.1.35 5.5 11 25°C, 3 h, stable. Gradual irreversible inactivation below pH 5.5 Homo sapiens