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Literature summary for 2.7.1.35 extracted from

  • Scott, T.C.; Phillips, M.A.
    Characterization of Trypanosoma brucei pyridoxal kinase: purification, gene isolation and expression in Escherichia coli (1997), Mol. Biochem. Parasitol., 88, 1-11.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Trypanosoma brucei

Inhibitors

Inhibitors Comment Organism Structure
pyridoxal 0.1 mM, substrate inhibition Trypanosoma brucei

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0091
-
ATP pH 7, 37°C Trypanosoma brucei
0.022
-
pyridoxal pH 7, 37°C Trypanosoma brucei
0.038
-
pyridoxal pH 7, 37°C, recombinant enzyme Trypanosoma brucei
0.127
-
ATP pH 7, 37°C, recombinant enzyme Trypanosoma brucei

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
37000
-
2 * 37000, enzyme exists as dimer in solution, SDS-PAGE Trypanosoma brucei
73000
-
gel filtration Trypanosoma brucei

Organism

Organism UniProt Comment Textmining
Trypanosoma brucei
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant enzyme Trypanosoma brucei

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.52
-
-
Trypanosoma brucei

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
dimer 2 * 37000, enzyme exists as dimer in solution, SDS-PAGE Trypanosoma brucei

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.4
-
pyridoxal pH 7, 37°C, recombinant enzyme Trypanosoma brucei