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Literature summary extracted from

  • Huang, S.; Ma, W.; Zhang, P.; Zhang, J.; Xie, Y.; Huang, L.
    Recombinant expression, purification and characterization of Bombyx mori (Lepidoptera: Bombycidae) pyridoxal kinase (2011), Eur. J. Entomol., 108, 25-34.
No PubMed abstract available

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.1.35 expressed in Escherichia coli Rosetta (DE3) cells Bombyx mori

General Stability

EC Number General Stability Organism
2.7.1.35 if instead of the phosphate buffer an acetate buffer is used, enzymatic activity is reduced to 74% and almost no activity is recorded when a citrate buffer is used Bombyx mori

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.1.35 0.0441
-
pyridoxal in 70 mM potassium phosphate (pH 5.5), 0.5 mM ZnCl2, at 37°C Bombyx mori
2.7.1.35 0.0579
-
ATP in 70 mM potassium phosphate (pH 5.5), 0.5 mM ZnCl2, at 37°C Bombyx mori

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.1.35 Ca2+
-
Bombyx mori
2.7.1.35 Co2+
-
Bombyx mori
2.7.1.35 Fe2+
-
Bombyx mori
2.7.1.35 K+ when only triethanolamine is present as the cation, K+ is an activator of the enzyme Bombyx mori
2.7.1.35 Mn2+
-
Bombyx mori
2.7.1.35 Zn2+ Zn2+ is the most effective cation for catalysis under saturating substrate concentrations Bombyx mori

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.7.1.35 33900
-
2 * 33900, SDS-PAGE Bombyx mori
2.7.1.35 68000
-
gel filtration Bombyx mori

Organism

EC Number Organism UniProt Comment Textmining
2.7.1.35 Bombyx mori Q1PCB1
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.1.35 Ni Sepharose affinity column chromatography Bombyx mori

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 0.07
-
crude enzyme, in 70 mM potassium phosphate (pH 5.5), 0.5 mM ZnCl2, at 37°C Bombyx mori
2.7.1.35 1.8
-
crude enzyme, in 70 mM potassium phosphate (pH 5.5), 0.5 mM ZnCl2, at 37°C Bombyx mori

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.1.35 ATP + pyridoxal
-
Bombyx mori ADP + pyridoxal 5'-phosphate
-
?

Subunits

EC Number Subunits Comment Organism
2.7.1.35 homodimer 2 * 33900, SDS-PAGE Bombyx mori

Synonyms

EC Number Synonyms Comment Organism
2.7.1.35 PLK
-
Bombyx mori

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.7.1.35 50
-
-
Bombyx mori

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
2.7.1.35 40
-
greatest stability is at below 40°C Bombyx mori

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.7.1.35 1.23
-
ATP in 70 mM potassium phosphate (pH 5.5), 0.5 mM ZnCl2, at 37°C Bombyx mori
2.7.1.35 1.35
-
pyridoxal in 70 mM potassium phosphate (pH 5.5), 0.5 mM ZnCl2, at 37°C Bombyx mori

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.7.1.35 5.5 6
-
Bombyx mori

pH Range

EC Number pH Minimum pH Maximum Comment Organism
2.7.1.35 4.5 8.5 the enzyme is inactive below pH 4.5. Enzyme activity decreases slowly above pH 6.0, to approximately 35% at pH 8.5 Bombyx mori

pI Value

EC Number Organism Comment pI Value Maximum pI Value
2.7.1.35 Bombyx mori calculated from amino acid sequence
-
6.3

General Information

EC Number General Information Comment Organism
2.7.1.35 physiological function pyridoxal kinase is a key enzyme in the metabolism of vitamin B6 Bombyx mori

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
2.7.1.35 21.2
-
ATP in 70 mM potassium phosphate (pH 5.5), 0.5 mM ZnCl2, at 37°C Bombyx mori
2.7.1.35 30.6
-
pyridoxal in 70 mM potassium phosphate (pH 5.5), 0.5 mM ZnCl2, at 37°C Bombyx mori