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Literature summary for 2.7.11.5 extracted from

  • Yates, S.P.; Edwards, T.E.; Bryan, C.M.; Stein, A.J.; Van Voorhis, W.C.; Myler, P.J.; Stewart, L.J.; Zheng, J.; Jia, Z.
    Structural basis of the substrate specificity of bifunctional isocitrate dehydrogenase kinase/phosphatase (2011), Biochemistry, 50, 8103-8106.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.7.11.5

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Escherichia coli
Mg2+ required Burkholderia pseudomallei

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + [isocitrate dehydrogenase (NADP+)] Burkholderia pseudomallei
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 ADP + [isocitrate dehydrogenase (NADP+)] phosphate
-
 r
ATP + [isocitrate dehydrogenase (NADP+)] Escherichia coli Escherichia coli AceK can cross-phosphorylate Burkholderia pseudomallei IDH ADP + [isocitrate dehydrogenase (NADP+)] phosphate
-
 r

Organism

Organism UniProt Comment Textmining
Burkholderia pseudomallei Q63Y16
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-
Escherichia coli
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-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + [isocitrate dehydrogenase (NADP+)]
-
 Burkholderia pseudomallei ADP + [isocitrate dehydrogenase (NADP+)] phosphate
-
 r
ATP + [isocitrate dehydrogenase (NADP+)] Escherichia coli AceK can cross-phosphorylate Burkholderia pseudomallei IDH Escherichia coli ADP + [isocitrate dehydrogenase (NADP+)] phosphate
-
 r
ATP + [isocitrate dehydrogenase (NADP+)] Ser113 from Escherichia coli class A ICDH is the target of phosphorylation by AceK and is structurally conserved among all ICDHs. Burkholderia pseudomallei class A ICDH also exhibits the necessary structural elements required for Escherichia coli AceK recognition Escherichia coli ADP + [isocitrate dehydrogenase (NADP+)] phosphate
-
 r
additional information AceK kinase assay is coupled to ICDH activity, whereby the reduction of NADP+ to NADPH is monitored. When AceK phosphorylates ICDH, the activity of ICDH is inhibited. Structure comparisons of Burkholderia pseudomallei ICDH and Echerichia coli ICDH substrates, overview. Bacillus subtilis ICDH and Acidithiobacillus thiooxidans ICDH are poor substrates for AceK Escherichia coli ?
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 ?

Synonyms

Synonyms Comment Organism
AceK
-
 Escherichia coli
AceK
-
 Burkholderia pseudomallei
bifunctional isocitrate dehydrogenase kinase/phosphatase
-
 Escherichia coli
bifunctional isocitrate dehydrogenase kinase/phosphatase
-
 Burkholderia pseudomallei

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Escherichia coli
ATP
-
 Burkholderia pseudomallei

General Information

General Information Comment Organism
evolution the highly stringent AceK binding sites on ICDH are maintained only in Gram-negative bacteria Escherichia coli
physiological function isocitrate dehydrogenase kinase/phosphatase, AceK, regulates entry into the glyoxylate bypass by reversibly phosphorylating isocitrate dehydrogenase, ICDH Escherichia coli