Amino acid sequence round the site of phosphorylation in isocitrate dehydrogenase from Escherichia coli ML308
- 20 August 1984
- journal article
- Published by Wiley in FEBS Letters
- Vol. 174 (1) , 112-115
- https://doi.org/10.1016/0014-5793(84)81087-x
Abstract
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.Keywords
This publication has 12 references indexed in Scilit:
- Isolation of active and inactive forms of isocitrate dehydrogenase from Escherichia coli ML308European Journal of Biochemistry, 1984
- Partial purification and properties of isocitrate dehydrogenase kinase/phosphatase from Escherichia coli ML308European Journal of Biochemistry, 1984
- The structure of the B subunit of calcineurinEuropean Journal of Biochemistry, 1984
- A comparison of the phosphorylated and unphosphorylated forms of isocitrate dehydrogenase from Escherichia coli ML308FEBS Letters, 1984
- Phosphorylation of isocitrate dehydrogenase as a demonstration of enhanced sensitivity in covalent regulationNature, 1983
- A protein with kinase and phosphatase activities involved in regulation of tricarboxylic acid cycleNature, 1982
- Primary structure of bovine complement activation fragment C4a, the third anaphylatoxin. Purification and complete amino acid sequenceBiochemical Journal, 1982
- Glycogen Synthase from Rabbit Skeletal MuscleEuropean Journal of Biochemistry, 1980
- Purification and properties of phosphorylated isocitrate dehydrogenase of Escherichia coli.Journal of Biological Chemistry, 1979
- Phosphorylation of Isocitrate Dehydrogenase of Escherichia coliScience, 1979