Affiliation:
1. Institute of Biotechnology, University of Cambridge, Cambridge CB2 1QT, United Kingdom
Abstract
ABSTRACT
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.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
Cited by
69 articles.
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