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Journal of Bacteriology, February 1999, p. 1030-1034, Vol. 181, No. 3
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

The udhA Gene of Escherichia coli Encodes a Soluble Pyridine Nucleotide Transhydrogenase

Birgitte Boonstra, Christopher E. French,dagger Ian Wainwright, and Neil C. Bruce*

Institute of Biotechnology, University of Cambridge, Cambridge CB2 1QT, United Kingdom

Received 9 September 1998/Accepted 16 November 1998

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.

* Corresponding author. Mailing address: Institute of Biotechnology, University of Cambridge, Tennis Court Rd., Cambridge CB2 1QT, United Kingdom. Phone: 44 1223 334168. Fax: 44 1223 334162. E-mail: N.Bruce{at}biotech.cam.ac.uk.

dagger Present address: Institute of Cell and Molecular Biology, University of Edinburgh, Edinburgh EH9 3JR, United Kingdom.

Journal of Bacteriology, February 1999, p. 1030-1034, Vol. 181, No. 3
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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