Pyrrolo-quinoline quinone (PQQ) is redox coenzyme, which serves as a cofactor
for a number of enzymes (quinoproteins) and particularly for some bacterial
dehydrogenases [1,2]. A number of these bacterial quinoproteins are clearly
evolutionary related. These proteins are listed below.
Methanol dehydrogenases (MDH) (EC 220.127.116.11), from methylotrophs.
Ethanol dehydrogenases from Acetobacter aceti .
Glucose dehydrogenase (EC 18.104.22.168) from Acinetobacter calcoaceticus,
Escherichia coli, and Gluconobacter oxydans .
These dehydrogenases all have from 600 to 800 amino acids. We developed two
signature patterns for these proteins using sequence data from well conserved
regions: the first one is located in the N-terminal half while the second one
is from the C-terminal half.
December 2004 / Patterns and text revised.
PROSITE methods (with tools and information) covered by this documentation:
Duine J.A. Jongejan J.A.
Quinoproteins, enzymes with pyrrolo-quinoline quinone as cofactor.
Cleton-Jansen A.-M. Dekker S. van de Putte P. Goosen N.
Mol. Gen. Genet. 229:206-212(1991).
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