Open AccessPhosphofructokinase: Complete Amino‐Acid Sequence of the Enzyme from Bacillus stearothermophilus
Author(s) -
KOLB Edith,
HUDSON Peter J.,
HARRIS J. Ieuan
Publication year - 1980
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1980.tb04754.x
Subject(s) - cyanogen bromide , peptide sequence , peptide , biochemistry , sequence (biology) , protein primary structure , phosphofructokinase , protein subunit , complete sequence , enzyme , biology , sequence analysis , proteolytic enzymes , chemistry , glycolysis , genome , gene
The entire amino acid sequence of the protein subunit of phosphofructokinase from Bacillus stearothermophilus has been established mainly by sequence analysis of cyanogen bromide fragments and of peptides derived from these fragments by further digestion with proteolytic enzymes. Overlaps of the cyanogen bromide fragments as well as peptide sequences necessary to complement and to confirm tentative assignments within the larger peptide fragments were obtained from the sequences of selected peptides isolated from tryptic and chymotryptic digests of the intact S ‐[ 14 C]‐carboxymethylated protein. Sequence information was also provided by automated sequence analysis of the intact protein subunit and of some of the larger peptide fragments. The sequence is as follows: