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Literature summary for 2.7.1.26 extracted from

  • Merrill, A.H.; McCormick, D.B.
    Preparation and properties of immobilized flavokinase (1979), Biotechnol. Bioeng., 21, 1629-1638.
    View publication on PubMed
Search for more literature for 2.7.1.26

Application

Application Comment Organism
synthesis immobilized enzyme is effective for phosphorylating riboflavin and numerous riboflavin analogs and provides a facile method for preparing exclusively other synthetic methods, the 5'-phosphates Rattus norvegicus

General Stability

General Stability Organism
enzyme immobilized by amide linkage to omega aminoalkyl-agarose-beads has a half-life of three weeks at 25°C Rattus norvegicus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.01
-
 riboflavin pH 8.0, 37°C Rattus norvegicus
0.2
-
 ATP pH 8, 37°C Rattus norvegicus

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
 Rattus norvegicus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + 2-thioriboflavin 30% of the activity with riboflavin Rattus norvegicus ADP + 2-thioriboflavin 5'-phosphate
-
 ?
ATP + 3-methylriboflavin 5% of the activity with riboflavin Rattus norvegicus ADP + 3-methylriboflavin 5'-phosphate
-
 ?
ATP + 5-deazariboflavin as active as riboflavin Rattus norvegicus ADP + 5-deazariboflavin 5'-phosphate
-
 ?
ATP + riboflavin
-
 Rattus norvegicus ADP + FMN
-
 ?
ATP + roseoflavin 90% of the activity with riboflavin Rattus norvegicus ADP + roseoflavin 5'-phosphate
-
 ?

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
25
-
 enzyme immobilized by amide linkage to omega aminoalkyl-agarose-beads has a half-life of three weeks Rattus norvegicus