Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.14.20.6 extracted from

  • Lin, G.Z.; Lian, Y.J.; Ryu, J.H.; Sung, M.K.; Park, J.S.; Park, H.J.; Park, B.K.; Shin, J.S.; Lee, M.S.; Cheon, C.I.
    Expression and purification of His-tagged flavonol synthase of Camellia sinensis from Escherichia coli (2007), Protein Expr. Purif., 55, 287-292.
    View publication on PubMed

Application

Application Comment Organism
synthesis production of active flavonol synthase from Camellia sinensis in Escherichia coli, with high specific activity Camellia sinensis

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli, His-tag Camellia sinensis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.139
-
dihydroquercetin pH 7.5, 30°C Camellia sinensis

Metals/Ions

Metals/Ions Comment Organism Structure
Iron presence of Fe2+ in purification buffer is required to yield active enzyme Camellia sinensis

Organism

Organism UniProt Comment Textmining
Camellia sinensis A2TJG2
-
-

Purification (Commentary)

Purification (Comment) Organism
from inclusion bodies of recombinant Escherichia coli, denaturation with 6 M urea. Addition of FeSO4 to purification buffers significantly improves the recovery of active enzyme Camellia sinensis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
dihydroquercetin + 2-oxoglutarate + O2
-
Camellia sinensis quercetin + succinate + CO2 + H2O
-
?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.16
-
dihydroquercetin pH 7.5, 30°C Camellia sinensis