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

BRENDA support

Literature summary 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

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

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.99.28 400
-
 fructose
-
 Zymomonas mobilis

Organism

EC Number Organism UniProt Comment Textmining
1.1.99.28 Zymomonas mobilis
-
-
-

Substrates and Products (Substrate)

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

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.1.99.28 35
-
 52 h, 10% loss of activity Zymomonas mobilis

Cofactor

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