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

BRENDA support

Literature summary for 1.1.5.2 extracted from

  • Ivanova, E.V.; Ershov, A.Y.; Laurinavicius, V.; Meskus, R.; Ryabov, A.D.
    Comparative kinetic study of D-glucose oxidation by ruthenium(III) compounds catalyzed by FAD-dependent glucose oxidase and PQQ-dependent glucose dehydrogenase (2003), Biochemistry, 68, 407-415.
    View publication on PubMed

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information kinetic study, enzyme follows Michaelis-Menten kinetics using artificial electron transfer mediator system based on ruthenium(III) compounds for activity assays Erwinia sp.

Organism

Organism UniProt Comment Textmining
Erwinia sp.
-
-
-

Reaction

Reaction Comment Organism Reaction ID
D-glucose + ubiquinone = D-glucono-1,5-lactone + ubiquinol catalytic mechanism Erwinia sp.

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
12
-
purified enzyme Erwinia sp.

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-glucose + ubiquinone
-
Erwinia sp. D-glucono-1,5-lactone + ubiquinol
-
?

Synonyms

Synonyms Comment Organism
PQQ-dependent GDH
-
Erwinia sp.
PQQ-dependent glucose dehydrogenase
-
Erwinia sp.

Cofactor

Cofactor Comment Organism Structure
additional information ruthenium(III) bispyridine compounds and ruthenium(III) 4-methyl-bispyridine compounds can act as artificial electron transfer mediator system Erwinia sp.
pyrroloquinoline quinone i.e. PQQ, dependent on Erwinia sp.