Molecular cloning and nucleotide sequence of the Corynebacterium glutamicum pheA gene

Abstract

The pheA gene of Corynebacterium glutamicum encoding prephenate dehydratase was isolated from a gene bank constructed in C. glutamicum. The specffic activity of prephenate dehydratase was increased six-fold in strains harboring the cloned gene. Genetic and strucetural 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.

Identification and analysis of genes from Streptomyces pristinaespiralis encoding enzymes involved in the biosynthesis of the 4‐dimethylamino‐l‐phenylalanine precursor of pristinamycin I

“…Different monofunctional chorismate mutases are found in prokaryotes, yeast and plants and probably represent the common ancestral mutase (Xia and Jensen, 1992). Prephenate dehydratases are also found as monofunctional enzymes, in B. subtilis ( Trach and Hoch, 1989) and Corynebacterium glutamicum (Follettie and Sinskey, 1986). No correlation could be made between the monofunctional activities of the enzymes and their involvement in primary or secondary metabolism.…”

Genetic separability of the chorismate mutase and prephenate dehydrogenase components of the Escherichia coli tyrA gene product

“…Support for this view comes from the sequence of a monofunctional prephenate dehydratase from Corynebacterium glutamicum which has homology only to the portion of pheA which is not homologous to tyrA (5).…”

Purification, cloning, and primary structure of an enantiomer-selective amidase from Brevibacterium sp. strain R312: structural evidence for genetic coupling with nitrile hydratase

“…(18). Brevibacterium genomic DNA was prepared as described previously (9). The Sequenase Version 2-0 (United States Biochemical Corp.) was used for DNA sequencing with [kx-355]dATP (Amersham Corp.).…”