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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Base Sequence
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Binding Sites
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Cloning, Molecular
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Escherichia coli / enzymology*
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Escherichia coli / genetics*
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Genome, Bacterial
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Molecular Sequence Data
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NADP Transhydrogenases / biosynthesis
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NADP Transhydrogenases / chemistry
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NADP Transhydrogenases / genetics*
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Recombinant Proteins / biosynthesis
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Recombinant Proteins / chemistry
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Sequence Alignment
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Sequence Homology, Amino Acid
Substances
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Recombinant Proteins
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NADP Transhydrogenases