Open AccessPrimary structures of Escherichia coli pyruvate formate‐lyase and pyruvate‐formate‐lyase‐activating enzyme deduced from the DNA nucleotide sequences
Author(s) -
RÖDEL Wolfgang,
PLAGA Wulf,
FRANK Rainer,
KNAPPE Joachim
Publication year - 1988
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1988.tb14356.x-i2
Subject(s) - lyase , nucleic acid sequence , biochemistry , escherichia coli , nucleotide , protein primary structure , enzyme , biology , formate , dna , peptide sequence , gene , chemistry , microbiology and biotechnology , catalysis
The structural gene of pyruvate formate‐lyase ( pfl ) and that of pyruvate‐formate‐lyase‐activating enzyme were shown to be adjacent on the chromosomal map of Escherichia coli . DNA sequencing was performed along a stretch of 3592 nucleotides to obtain the amino acid sequences of both proteins. The derived primary structures (759 and 245 residues) were confirmed by partial structure analyses on the purified proteins. The open reading frames are separated by a 194‐nucleotide stretch, and their flanking regions include signal elements that are compatible with separate control of protein synthesis from the two genes.