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

BRENDA support

Literature summary for 1.1.99.35 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
Search for more literature for 1.1.99.35

Metals/Ions

Metals/Ions Comment Organism Structure
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

Organism UniProt Comment Textmining
Acinetobacter calcoaceticus P05465
-
-

Synonyms

Synonyms Comment Organism
soluble PQQ-dependent glucose dehydrogenase
-
 Acinetobacter calcoaceticus

Cofactor

Cofactor Comment Organism Structure
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