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Literature summary for 1.1.99.28 extracted from

  • Furlinger, M.; Nidetzky, B.; Scopes, R.K.; Haltrich, D.; Kulbe, K.D.
    Inactivation of glucose-fructose oxidoreductase from Zymomonas mobilis during its catalytic action (1996), Ann. N. Y. Acad. Sci., 799, 752-756.
No PubMed abstract available

General Stability

General Stability Organism
in absence of substrates or in presence of only one substrate, either fructose or glucose, the enzyme is fully stable Zymomonas mobilis
thiol reagents stabilize. Dithiothreitol is the most efficient, 5-15 mM Zymomonas mobilis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
400
-
fructose
-
Zymomonas mobilis

Organism

Organism UniProt Comment Textmining
Zymomonas mobilis
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-glucose + D-fructose
-
Zymomonas mobilis D-glucono-1,5-lactone + D-sorbitol
-
?

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
35
-
52 h, 10% loss of activity Zymomonas mobilis

Cofactor

Cofactor Comment Organism Structure
NADP+ tightly bound as hydrogen carrier Zymomonas mobilis
NADPH tightly bound as hydrogen carrier Zymomonas mobilis