Molecular cloning and nucleotide sequence of the Corynebacterium glutamicum pheA gene.

TitleMolecular cloning and nucleotide sequence of the Corynebacterium glutamicum pheA gene.
Publication TypeJournal Article
Year of Publication1986
AuthorsFollettie, MT, Sinskey, AJ
JournalJ Bacteriol
Date Published1986 Aug
KeywordsAmino Acid Sequence, Base Sequence, Chorismate Mutase, Cloning, Molecular, Codon, Corynebacterium, DNA, Bacterial, Escherichia coli, Genes, Genes, Bacterial, Genetic Complementation Test, Hydro-Lyases, Prephenate Dehydratase, Sequence Homology, Nucleic Acid

The pheA gene of Corynebacterium glutamicum encoding prephenate dehydratase was isolated from a gene bank constructed in C. glutamicum. The specific activity of prephenate dehydratase was increased six-fold in strains harboring the cloned gene. Genetic and structural evidence is presented which indicates that prephenate dehydratase and chorismate mutase were catalyzed by separate enzymes in this species. The C. glutamicum pheA gene, subcloned in both orientations with respect to the Escherichia coli vector pUC8, was able to complement an E. coli pheA auxotroph. The nucleotide sequence of the C. glutamicum pheA gene predicts a 315-residue protein product with a molecular weight of 33,740. The deduced protein product demonstrated sequence homology to the C-terminal two-thirds of the bifunctional E. coli enzyme chorismate mutase-P-prephenate dehydratase.

Alternate JournalJ Bacteriol
Citation Key96
PubMed ID3525519
PubMed Central IDPMC212945