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Literature summary for 2.7.1.35 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)

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

General Stability

General Stability Organism
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]

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

Metals/Ions

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

Molecular Weight [Da]

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

Organism

Organism UniProt Comment Textmining
Bombyx mori Q1PCB1
-
-

Purification (Commentary)

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

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.07
-
crude enzyme, in 70 mM potassium phosphate (pH 5.5), 0.5 mM ZnCl2, at 37°C Bombyx mori
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)

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

Subunits

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

Synonyms

Synonyms Comment Organism
PLK
-
Bombyx mori

Temperature Optimum [°C]

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

Temperature Stability [°C]

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

Turnover Number [1/s]

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

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5.5 6
-
Bombyx mori

pH Range

pH Minimum pH Maximum Comment Organism
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

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

General Information

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

kcat/KM [mM/s]

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