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

BRENDA support

Literature summary extracted from

  • Olsthoorn, A.J.J.; Otsuki, T.; Duine, J.A.
    Negative cooperativity in the steady-state kinetics of sugar oxidation by soluble quinoprotein glucose dehydrogenase from Acinetobacter calcoaceticus (1998), Eur. J. Biochem., 255, 255-261.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.1.99.35 D-glucose
-
Acinetobacter calcoaceticus
1.1.99.35 lactose
-
Acinetobacter calcoaceticus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.99.35 additional information
-
additional information under conditions that avoid its masking by sugar-substrate inhibition as much as possible, negative kinetic cooperativity with respect to sugar substrate oxidation is observed. The cooperativity effect dramatically changes the performance of soluble GDH, as reflected by the V2 and K2 values for glucose in phosphate buffer being about 10-fold and 100-fold higher than the V1 and K1 values, respectively. Substituting the Ca2+ involved in activation of pyrroloquinoline quinone in soluble GDH by Sr2+ affects the cooperativity effect but not the two turnover rates of the hybrid enzyme for glucose Acinetobacter calcoaceticus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.1.99.35 Ca2+ substituting the Ca2+ involved in activation of pyrroloquinoline quinone in soluble GDH by Sr2+ affects the cooperativity effect but not the two turnover rates of the hybrid enzyme for glucose Acinetobacter calcoaceticus
1.1.99.35 Sr2+ substituting the Ca2+ involved in activation of pyrroloquinoline quinone in soluble GDH by Sr2+ affects the cooperativity effect but not the two turnover rates of the hybrid enzyme for glucose Acinetobacter calcoaceticus

Organism

EC Number Organism UniProt Comment Textmining
1.1.99.35 Acinetobacter calcoaceticus
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.1.99.35 D-glucose + acceptor = D-glucono-1,5-lactone + reduced acceptor ping-pong behaviour and double-substrate inhibition Acinetobacter calcoaceticus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.99.35 D-galactose + oxidized N-methylphenazonium methyl sulfate
-
Acinetobacter calcoaceticus D-galactono-1,5-lactone + reduced N-methylphenazonium methyl sulfate
-
?
1.1.99.35 D-glucose + oxidized N-methylphenazonium methyl sulfate
-
Acinetobacter calcoaceticus D-glucono-1,5-lactone + reduced N-methylphenazonium methyl sulfate
-
?
1.1.99.35 D-xylose + oxidized N-methylphenazonium methyl sulfate
-
Acinetobacter calcoaceticus D-xylono-1,5-lactone + reduced N-methylphenazonium methyl sulfate
-
?
1.1.99.35 lactose + oxidized N-methylphenazonium methyl sulfate
-
Acinetobacter calcoaceticus 4-O-beta-D-galactopyranosyl-D-glucono-1,5-lactone + reduced N-methylphenazonium methyl sulfate
-
?

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
1.1.99.35 61
-
lactose pH 7.0, 20°C Acinetobacter calcoaceticus
1.1.99.35 92
-
D-glucose pH 7.0, 20°C Acinetobacter calcoaceticus
1.1.99.35 156
-
D-glucose enzyme containing Sr2+ instead of Ca2+, pH 7.0, 20°C Acinetobacter calcoaceticus