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Biochemistry. 2011 Sep 27;50(38):8103-6. doi: 10.1021/bi200809p. Epub 2011 Sep 2.

Structural basis of the substrate specificity of bifunctional isocitrate dehydrogenase kinase/phosphatase.

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1
Department of Biomedical and Molecular Sciences, Queen's University, Kingston, ON K7L 3N6, Canada.

Abstract

Isocitrate dehydrogenase kinase/phosphatase (AceK) regulates entry into the glyoxylate bypass by reversibly phosphorylating isocitrate dehydrogenase (ICDH). On the basis of the recently determined structure of the AceK-ICDH complex from Escherichia coli, we have classified the structures of homodimeric NADP(+)-ICDHs to rationalize and predict which organisms likely contain substrates for AceK. One example is Burkholderia pseudomallei (Bp). Here we report a crystal structure of Bp-ICDH that exhibits the necessary structural elements required for AceK recognition. Kinetic analyses provided further confirmation that Bp-ICDH is a substrate for AceK. We conclude that the highly stringent AceK binding sites on ICDH are maintained only in Gram-negative bacteria.

PMID:
21870819
PMCID:
PMC3354702
DOI:
10.1021/bi200809p
[Indexed for MEDLINE]
Free PMC Article
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