Cloning of cDNA encoding the bifunctional dehydroquinase.shikimate dehydrogenase of aromatic-amino-acid biosynthesis in Nicotiana tabacum.
Biochem J, 1994/8/15;302 ( Pt 1):11-4.
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PMID: 8067995
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Abstract
Nicotiana tabacum cDNA encoding a bifunctional protein having catalytic domains for dehydroquinase and shikimate dehydrogenase was cloned and sequenced. Complementation of Escherichia coli aroD and aroE auxotrophs was successful. Amino acid sequencing located the N-terminus of the mature protein. The two catalytic domains exhibited greater amino acid identity with prokaryote homologues than with yeast and fungal homologues.
MeSH terms
Alcohol Oxidoreductases; Amino Acid Sequence; Amino Acids; Base Sequence; Cloning, Molecular; DNA, Complementary; Escherichia coli; Molecular Sequence Data; Plants, Toxic; Sequence Homology, Amino Acid; Nicotiana
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