1.1.99.35	pyrroloquinoline quinone	-	723943, 724172, 724836, 724852, 739848, 739872, 739873, 739914, 762778, 762834, 762923	
1.1.99.35	pyrroloquinoline quinone	crystallization data	639204	
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	762554	
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	702726	
1.1.99.35	pyrroloquinoline quinone	the catalytic potential of the cofactor in the enzyme is not determined by its adduct-forming ability but by whether it is or can be activated with Ca2+	702202