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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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A single amino acid substitution changes the substrate specificity of quinoprotein glucose dehydrogenase in Gluconobacter oxydans.

Gluconobacter oxydans contains pyrroloquinoline quinone-dependent glucose dehydrogenase ( GDH). Two isogenic G. oxydans strains, P1 and P2, which differ in their substrate specificity with respect to oxidation of sugars have been analysed. P1 can oxidize only D-glucose, whereas P2 is also capable of the oxidation of the disaccharide maltose. To investigate the nature of this maltose-oxidizing property we cloned the gene encoding GDH from P2. Expression of P2 gdh in P1 enables the latter strain to oxidize maltose, indicating that a mutation in the P2 gdh gene is responsible for the change in substrate specificity. This mutation could be ascribed to a 1 bp substitution resulting in the replacement of His 787 by Asn.[1]

References

  1. A single amino acid substitution changes the substrate specificity of quinoprotein glucose dehydrogenase in Gluconobacter oxydans. Cleton-Jansen, A.M., Dekker, S., van de Putte, P., Goosen, N. Mol. Gen. Genet. (1991) [Pubmed]
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