CLONING OF CDNA-ENCODING THE BIFUNCTIONAL DEHYDROQUINASE-CENTER-DOT-SHIKIMATE DEHYDROGENASE OF AROMATIC-AMINO-ACID BIOSYNTHESIS IN NICOTIANA-TABACUM

Nicotiana tabacum cDNA encoding a bifunctional protein having catalyti c domains for dehydroquinase and shikimate dehydrogenase was cloned an d sequenced. Complementation of Escherichia coli aroD and aroE auxotro phs was successful. Amino acid sequencing located the N-terminus of th e mature protein. The two catalytic domains exhibited greater amino ac id identity with prokaryote homologues than with yeast and fungal homo logues.