Isolation and Anlaysis of the aroE Gene Encoding Shikimate Dehydrogenase from Corynebacterium glutamicum

Abstract

The aroE gene was cloned from Corynebacterium glutamicum by complementation of an Escherichia coli aromatic amino acid auxotroph. The E. coli aroE gene codes for shikimate dehydrogenase, an enzyme involved in the aromatic amino acid biosynthetic pathway. The cloned DNA fragment in the recombinant plasmid, named pROE1, was physically mapped with several restriction endonucleases. We determined the DNA nucleotide sequences of the DNA fragment and reported here the sequences of the aroE gene. The complete nucleotide sequences of the aroE gene showed an open reading frame encoding a protein of 274 amino acids. Comparison of this deduced amino acid sequences of C. glutamicum aroE gene with those of the enzyme from Mycobacterium tuberculosis, Archaeoglobos folgidus and Synechocystis sp. revealed 45%, 32% and 28% similarity, respectively.