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Literature summary for 2.7.11.5 extracted from

  • Zheng, J.; Yates, S.P.; Jia, Z.
    Structural and mechanistic insights into the bifunctional enzyme isocitrate dehydrogenase kinase/phosphatase AceK (2012), Philos. Trans. R. Soc. Lond. B Biol. Sci., 367, 2656-2668.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.7.11.5

Protein Variants

Protein Variants Comment Organism
D475A the mutation in this signature motif completely abolishes kinase activity of the enzyme Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required, only one Mg2þ is found in AceK, whereas two are present in ePKs Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + [isocitrate dehydrogenase (NADP+)] Escherichia coli Escherichia coli AceK can cross-phosphorylate Burkholderia pseudomallei IDH ADP + [isocitrate dehydrogenase (NADP+)] phosphate
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 r
additional information Escherichia coli AceK is a bifunctional enzyme, that phosphorylates and dephosphorylates isocitrate dehydrogenase with its unique active site that harbours both the kinase and ATP/ADP-dependent phosphatase activities ?
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 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
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-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + [isocitrate dehydrogenase (NADP+)]
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 Escherichia coli ADP + [isocitrate dehydrogenase (NADP+)] phosphate
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 r
ATP + [isocitrate dehydrogenase (NADP+)] Escherichia coli AceK can cross-phosphorylate Burkholderia pseudomallei IDH Escherichia coli ADP + [isocitrate dehydrogenase (NADP+)] phosphate
-
 r
additional information AceK is a bifunctional enzyme, that phosphorylates and dephosphorylates isocitrate dehydrogenase with its unique active site that harbours both the kinase and ATP/ADP-dependent phosphatase activities Escherichia coli ?
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 ?
additional information AceK exhibits ATPase activity Escherichia coli ?
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 ?

Synonyms

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

Cofactor

Cofactor Comment Organism Structure
ADP AceK is strictly ATP/ADP-dependent Escherichia coli
ATP AceK is strictly ATP/ADP-dependent. Conserved Lys336 in the ATP binding site interacts with and stabilizes the alpha-phosphate of enzyme-bound ATP Escherichia coli

General Information

General Information Comment Organism
evolution the N-terminal domain or regulatory domain of AceK represents a unique protein fold with no structural homologues All known and putative AceK proteins exist only in Gram-negative bacteria, close evolutionary relationship among Gram-negative bacterial AceK-IDH systems Escherichia coli
metabolism AceK controls the switch between the Krebs cycle and the glyoxylate bypass via regulation of isocitrate dehydrogenase through inactivating phosphorylation and activating dephosphorylation, pathway overview Escherichia coli
additional information AceK and its complex with its protein substrate isocitrate dehydrogenase, IDH, interaction analysis, overview. Asp457-Asn462-Asp475 catalytic triad. In addition to this catalytic element, a phosphotransferase motif is also evident in AceK with sequence is 455PGDMLFKNFGV465. One of the most striking differences between AceK and the eukaryotic protein kinases family is the presence of loop beta3aalphaC in AceK. This regulatory loop shields and exposes ATP in the AMP-bound and AMP-free AceK structures, respectively, thereby acting as a regulator of catalytic function as it controls the accessibility to the ATP binding site. The regulatory domain of AceK contains binding pockets for small molecules that can regulate the function of the catalytic kinase domain of AceK Escherichia coli
physiological function AceK controls the switch between the Krebs cycle and the glyoxylate bypass via regulation of isocitrate dehydrogenase through inactivating phosphorylation and activating dephosphorylation Escherichia coli