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Literature summary extracted from

  • Stines-Chaumeil, C.; Mavre, F.; Kauffmann, B.; Mano, N.; Limoges, B.
    Mechanism of reconstitution/activation of the soluble PQQ-dependent glucose dehydrogenase from Acinetobacter calcoaceticus a comprehensive study (2020), ACS Omega, 5, 2015-2026 .
    View publication on PubMedView publication on EuropePMC

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.1.99.35 Ca2+ reconstitution mechanism of the enzyme (sGDH) with its two cofactors, i.e., pyrroloquinoline quinone (PQQ) and Ca2+: pyrroloquinoline quinone first binds to apo-sGDH, it strongly impedes the access of Ca2+ to its enclosed position at the bottom of the enzyme binding site, thereby greatly slowing down the reconstitution rate of sGDH. The slow calcium insertion may purposely be accelerated by providing more flexibility to the Ca2+ binding loop through the specific mutation of the calcium-coordinating P248 proline residue, reducing thus the kinetic barrier to calcium ion insertion Acinetobacter calcoaceticus

Organism

EC Number Organism UniProt Comment Textmining
1.1.99.35 Acinetobacter calcoaceticus P05465
-
-

Synonyms

EC Number Synonyms Comment Organism
1.1.99.35 soluble PQQ-dependent glucose dehydrogenase
-
Acinetobacter calcoaceticus

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.99.35 pyrroloquinoline quinone reconstitution mechanism of the enzyme (sGDH) with its two cofactors, i.e., pyrroloquinoline quinone (PQQ) and Ca2+: pyrroloquinoline quinone first binds to apo-sGDH, it strongly impedes the access of Ca2+ to its enclosed position at the bottom of the enzyme binding site, thereby greatly slowing down the reconstitution rate of sGDH. The slow calcium insertion may purposely be accelerated by providing more flexibility to the Ca2+ binding loop through the specific mutation of the calcium-coordinating P248 proline residue, reducing thus the kinetic barrier to calcium ion insertion Acinetobacter calcoaceticus