Ontology highlight
ABSTRACT:
SUBMITTER: Boonstra B
PROVIDER: S-EPMC93474 | biostudies-literature | 1999 Feb
REPOSITORIES: biostudies-literature
Boonstra B B French C E CE Wainwright I I Bruce N C NC
Journal of bacteriology 19990201 3
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. ...[more]