Abstract / Description of output
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.
| Original language | English |
|---|---|
| Pages (from-to) | 1030-1034 |
| Number of pages | 5 |
| Journal | Journal of Bacteriology |
| Volume | 181 |
| Issue number | 3 |
| Publication status | Published - Feb 1999 |