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Literature summary for extracted from

  • Oubrie, A.; Rozeboom, H.J.; Dijkstra, B.W.
    Active-site structure of the soluble quinoprotein glucose dehydrogenase complexed with methylhydrazine: A covalent cofactor-inhibitor complex (1999), Proc. Natl. Acad. Sci. USA, 96, 11787-11791.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
ternary complex of s-GDH with PQQ and methylhydrazine, at 1.5 A resolution. Formation of a covalent PQQ adduct in the active-site. The C5 carbonyl group of the cofactor is the most reactive moiety of PQQ. The binding of the cofactor to s-GDH is predominantly governed by polar interactions. The C2, C7, and C9 carboxyl groups of PQQ form salt bridges with Arg408, Lys377, and Arg406, respectively. The ortho-quinone O4 and O5 atoms are bound by Asn229 and Arg228, respectively. The N6, O7A, and O5 atoms of PQQ are ligands for the active-site calcium ion. The other calcium ligands are provided by the two main chain carbonyl oxygen atoms of Gly-247 and Pro-248 and two watermolecules Acinetobacter calcoaceticus


Inhibitors Comment Organism Structure
methylhydrazine competitive inhibitor Acinetobacter calcoaceticus


Organism UniProt Comment Textmining
Acinetobacter calcoaceticus


Synonyms Comment Organism
Acinetobacter calcoaceticus