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PMID: 6381094 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Amino acid sequence round the site of phosphorylation in isocitrate dehydrogenase from Escherichia coli ML308.

FEBS letters ·Vol. 174 ·No. 1 ·1984-08-20 ·Pages 112-5

Borthwick AC, Holms WH, Nimmo HG

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.

MeSH Terms
Amino Acid Sequence Chymotrypsin Escherichia coli/enzymology Isocitrate Dehydrogenase/metabolism Kinetics Peptide Fragments/analysis Phosphopeptides/analysis Phosphorylation Thermolysin
Chemicals
Peptide Fragments Phosphopeptides Isocitrate Dehydrogenase Chymotrypsin Thermolysin
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Borthwick A C
Holms W H
Nimmo H G
Article Info
Journal
FEBS letters
Abbr.
FEBS Lett
ISSN
0014-5793
DOI
10.1016/0014-5793(84)81087-x
Published
1984-08-20
Pages
112-5
Language
English
Region
England
NLM ID
0155157
Subset
IM
External Links
PubMed source DOI: 10.1016/0014-5793(84)81087-x View journal details
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