Literature summary for 2.7.11.5 extracted from

Cozzone, A.J.; El-Mansi, M.
Control of isocitrate dehydrogenase catalytic activity by protein phosphorylation in Escherichia coli (2005), J. Mol. Microbiol. Biotechnol., 9, 132-146.

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Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
phosphoprotein	reversible inactivation of the enzyme is due to reversible phosphorylation catalyzed by ICDH kinase/phosphatase. This activity requires ATP. Phosphorylation of the Ser113 residue renders the enzyme catalytically inactive as it prevents isocitrate from binding to the active site. This is a consequence of the negative charge carried on phosphoserine 113 and the conformational change associated with it. The ICDH molecule readily undergoes domain shift and/or induced-fit conformational changes to accomodate the binding changes of ICDH kinase/phosphatase	Escherichia coli

Synonyms

Synonyms	Comment	Organism
ICDH	-	Escherichia coli

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Release 2023.1 (January 2023)