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Amino acid sequence round the site of phosphorylation in isocitrate dehydrogenase from Escherichia coli ML308
Author(s) -
Borthwick A.C.,
Holms W.H.,
Nimmo H.G.
Publication year - 1984
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(84)81087-x
Subject(s) - isocitrate dehydrogenase , escherichia coli , biochemistry , phosphorylation , peptide sequence , sequence (biology) , biology , chemistry , microbiology and biotechnology , enzyme , gene
Isocitrate dehydrogenase from Escherichia coli is regulated by a reversible phosphorylation mechanism. We report here the amino acid sequence round the phosphorylation site; this is the first such sequence to be reported for a bacterial protein kinase. The sequence does not resemble sequences phosphorylated by cyclic AMP‐dependent protein kinase.