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 .
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 |
|