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Literature summary extracted from

  • Matsushita, K.; Toyama, H.; Ameyama, M.; Adachi, O.; Dewanti, A.; Duine, J.A.
    Soluble and membrane-bound quinoprotein D-glucose dehydrogenases of the Acinetobacter calcoaceticus: the binding process of PQQ to the apoenzymes (1995), Biosci. Biotechnol. Biochem., 59, 1548-1555.
No PubMed abstract available

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.1.99.35 Ca2+ or Cd2+, Sr2+, or Mn2+, required for binding of cofactor PQQ in soluble isoform sGDH, 100% activity with Ca2+. Mg2+, or Ca2+, Zn2+, or Sr2+, required for binding of cofactor PQQ in membrane-bound isoform mGDH. 100% activity with Ca2+ Acinetobacter calcoaceticus
1.1.99.35 Cd2+ or Ca2+, Sr2+, or Mn2+, required for binding of cofactor PQQ in soluble isoform sGDH. Mg2+, or Ca2+, Zn2+, or Sr2+, required for binding of cofactor PQQ in membrane-bound isoform mGDH Acinetobacter calcoaceticus
1.1.99.35 Mg2+ or Ca2+, Zn2+, or Sr2+, required for binding of cofactor PQQ in membrane-bound isoform mGDH. With Mg2+, 115% of the activity with Ca2+ Acinetobacter calcoaceticus
1.1.99.35 Mn2+ or Ca2+, Sr2+, or Cd2+, required for binding of cofactor PQQ in soluble isoform sGDH. Mg2+, or Ca2+, Zn2+, or Sr2+, required for binding of cofactor PQQ in membrane-bound isoform mGDH Acinetobacter calcoaceticus
1.1.99.35 Sr2+ or Ca2+, Cd2+, or Mn2+, required for binding of cofactor PQQ in soluble isoform sGDH, with Sr2+, 67% of the activity with Ca2+. Mg2+, or Ca2+, Zn2+, or Sr2+, required for binding of cofactor PQQ in membrane-bound isoform mGDH, with Sr2+, 70% of the activity with Ca2+ Acinetobacter calcoaceticus

Organism

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

Synonyms

EC Number Synonyms Comment Organism
1.1.99.35 mGDH
-
Acinetobacter calcoaceticus

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.99.35 pyrroloquinoline quinone soluble isoform sGDH is able to bind two mol of PQQ in one mol of the homodimer with high affinity. The binding reaction is much faster at alkaline pH than at acidic pH and requires the presence of some divalent cations such as Cd2+, Ca2+, Sr2+, or Mn2+. Membrane-bound isoform mGDH binds one mol of PQQ in the monomeric enzyme with a relatively slow reaction process, which has an optimim at acidic pH and in the presence of divalent cations such as Mg2+, Ca2+, Zn2+, Sr2+. Binding of PQQ affects the conformation of both isoforms Acinetobacter calcoaceticus