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Literature summary extracted from

  • Marcinkeviciene, J.; Johansson, G.
    Kinetic studies of the active sites functioning in the quinohemoprotein fructose dehydrogenase (1993), FEBS Lett., 318, 23-26.
    View publication on PubMed

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.5.14 0.0011
-
 ferricyanide slow reaction phase Gluconobacter sp.
1.1.5.14 0.47
-
 ferricyanide slow reaction phase Gluconobacter sp.
1.1.5.14 4.2
-
 fructose slow reaction phase Gluconobacter sp.
1.1.5.14 11.8
-
 fructose fast reaction phase Gluconobacter sp.

Organism

EC Number Organism UniProt Comment Textmining
1.1.5.14 Gluconobacter sp.
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.1.5.14 D-fructose + acceptor = 5-dehydro-D-fructose + reduced acceptor ping-pong mechanism Gluconobacter sp.
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.5.14 D-fructose + ferricyanide
-
 Gluconobacter sp. 5-dehydro-D-fructose + ferrocyanide
-
 ?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.1.5.14 93
-
 ferricyanide slow reaction phase Gluconobacter sp.
1.1.5.14 95
-
 D-fructose slow reaction phase Gluconobacter sp.
1.1.5.14 162
-
 ferricyanide fast reaction phase Gluconobacter sp.
1.1.5.14 250
-
 D-fructose fast reaction phase Gluconobacter sp.

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.5.14 heme quinohemoprotein. Enzyme has two active centers: cytochrome c and pyrroloquinoline quinone Gluconobacter sp.
1.1.5.14 pyrroloquinoline quinone quinohemoprotein. Enzyme has two active centers: cytochrome c and pyrroloquinoline quinone Gluconobacter sp.