The udhA gene of Escherichia coli encodes a soluble pyridine nucleotide transhydrogenase

J Bacteriol. 1999 Feb;181(3):1030-4. doi: 10.1128/JB.181.3.1030-1034.1999.


The udhA gene of Escherichia coli was cloned and expressed in E. coli and found to encode an enzyme with soluble pyridine nucleotide transhydrogenase activity. The N-terminal end of the enzyme contains the fingerprint motif of a dinucleotide binding domain, not present in published E. coli genome sequences due to a sequencing error. E. coli is hereby the first organism reported to possess both a soluble and a membrane-bound pyridine nucleotide transhydrogenase.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Base Sequence
  • Binding Sites
  • Cloning, Molecular
  • Escherichia coli / enzymology*
  • Escherichia coli / genetics*
  • Genome, Bacterial
  • Molecular Sequence Data
  • NADP Transhydrogenases / biosynthesis
  • NADP Transhydrogenases / chemistry
  • NADP Transhydrogenases / genetics*
  • Recombinant Proteins / biosynthesis
  • Recombinant Proteins / chemistry
  • Sequence Alignment
  • Sequence Homology, Amino Acid


  • Recombinant Proteins
  • NADP Transhydrogenases