title: Cloning of cDNA encoding the bifunctional dehydroquinase.shikimate dehydrogenase of aromatic-amino-acid biosynthesis in Nicotiana tabacum.
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.
authors.affiliation: Department of Microbiology and Cell Science, University of Florida, Gainesville 32611-0100.
authors.forename: C A
authors.initials: CA
authors.lastname: Bonner
authors.forename: R A
authors.initials: RA
authors.lastname: Jensen
mesh_terms: D000429:Alcohol Oxidoreductases / Q000235:genetics*; D000595:Amino Acid Sequence; D000596:Amino Acids / Q000096:biosynthesis*; D001483:Base Sequence; D003001:Cloning, Molecular; D018076:DNA, Complementary; D004926:Escherichia coli / Q000235:genetics; D008969:Molecular Sequence Data; D010947:Plants, Toxic; D017386:Sequence Homology, Amino Acid; D014026:Nicotiana / Q000201:enzymology* / Q000378:metabolism
chemical_list: D000596:Amino Acids; D018076:DNA, Complementary; D000429:Alcohol Oxidoreductases; C022641:Shikimate dehydrogenase