Literature summary for 1.1.99.35 extracted from

Dewanti, A.R.; Duine, J.A.
Ca2+-assisted, direct hydride transfer, and rate-determining tautomerization of C5-reduced PQQ to PQQH2, in the oxidation of beta -D-glucose by soluble, quinoprotein glucose dehydrogenase (2000), Biochemistry, 39, 9384-9392.

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Organism

Organism	UniProt	Comment	Textmining
Acinetobacter calcoaceticus	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	the sequential steps in the mechanism of sGDH must be reversible substrate binding, direct transfer of a hydride ion (reversible or irreversible) from the C1 position of the beta-anomer of glucose to the C5 of PQQ, irreversible, rate-determining tautomerization of the fluorescing, C5-reduced PQQ to PQQH2 and release (or earlier) of the product, D-glucono-delta-lactone, and oxidation of PQQH2 by an electron acceptor. The PQQ-activating Ca2+ greatly facilitates the reactions occurring in the second step. His144 may also play a role in this by acting as a general base catalyst, initiating hydride transfer by abstracting a proton from the anomeric OH group of glucose	Acinetobacter calcoaceticus	?	-	?

Cofactor

Cofactor	Comment	Organism	Structure
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+	Acinetobacter calcoaceticus

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Release 2023.1 (January 2023)