Cloning of a Serratia marcescens DNA fragment that induces quinoprotein glucose dehydrogenase-mediated gluconic acid production in Escherichia coli in the presence of stationary phase Serratia marcescens

FEMS Microbiol Lett. 2001 Dec 18;205(2):215-20. doi: 10.1111/j.1574-6968.2001.tb10950.x.


Serratia marcescens ER2 was isolated from an endorhizosphere sample based on its high level of mineral phosphate solubilizing (MPS) activity. This phenotype was correlated with expression of the direct oxidation pathway. An ER2 plasmid library constructed in Escherichia coli strain DH5alpha was screened for MPS activity. A recombinant clone DH5alpha (pKG3791) was capable of gluconic acid (GA) production and tricalcium phosphate solubilization but only in the presence of stationary phase ER2 cells. GA production in DH5alpha (pKG3791) was apparently the result of the quinoprotein glucose dehydrogenase activity because AG121 (a Tn5 knockout of gcd) carrying pKG3791 did not produce GA under the same conditions. GA production by DH5alpha (pKG3791) was not observed when ER2 was replaced by another PQQ-producing strain bacterium. These data add to a growing body of evidence that E. coli contains some type of PQQ biosynthesis pathway distinct from those previously characterized in Gram-negative bacteria and that these genes may be induced under appropriate conditions.

Publication types

  • Comparative Study

MeSH terms

  • Calcium Phosphates / metabolism
  • Escherichia coli / genetics*
  • Escherichia coli / metabolism
  • Gluconates / metabolism
  • Glucose Dehydrogenases / biosynthesis
  • Glucose Dehydrogenases / genetics*
  • Molecular Sequence Data
  • Recombinant Proteins / biosynthesis
  • Serratia marcescens / enzymology
  • Serratia marcescens / genetics*


  • Calcium Phosphates
  • Gluconates
  • Recombinant Proteins
  • beta-tricalcium phosphate
  • Glucose Dehydrogenases
  • glucose dehydrogenase (pyrroloquinoline-quinone)
  • tricalcium phosphate
  • gluconic acid

Associated data

  • GENBANK/AY028915