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

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