EC Number   |
General Information |
Reference |
|---|
   2.7.11.5 | evolution |
AceK is significantly larger than typical eukaryotic protein kinases. Apart from the ATP-binding motif, AceK does not share sequence homology with any eukaryotic protein kinase or phosphatase |
-, 723265 |
| 2.7.11.5 | evolution |
the highly stringent AceK binding sites on ICDH are maintained only in Gram-negative bacteria |
721649 |
| 2.7.11.5 | 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 |
723346 |
| 2.7.11.5 | 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 |
723346 |
| 2.7.11.5 | metabolism |
Escherichia coli isocitrate dehydrogenase kinase/phosphatase is a unique bifunctional enzyme that phosphorylates or dephosphorylates isocitrate dehydrogenase, ICDH, in response to environmental changes, resulting in the inactivation or, respectively, activation of ICDH1. ICDH inactivation short-circuits the Krebs cycle by enabling the glyoxlate bypass |
-, 723265 |
| 2.7.11.5 | more |
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 |
723346 |
| 2.7.11.5 | more |
structures of AceK and its complex with ICDH. AceK contains a eukaryotic protein-kinase-like domain containing ATP and a regulatory domain with a distinct fold. AMP-mediated conformational change exposes and shields ATP, acting as a switch between AceK kinase and phosphatase activities, and ICDH-binding induces further conformational change for AceK activation. The substrate recognition loop of AceK binds to the ICDH dimer, allowing higher order substrate recognition and interaction, and inducing critical conformational change at the phosphorylation site of ICDH, structure-based recognition of Asp 477 being located at the ATP-binding site |
-, 723265 |
| 2.7.11.5 | 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 |
723346 |
| 2.7.11.5 | physiological function |
isocitrate dehydrogenase kinase/phosphatase, AceK, regulates entry into the glyoxylate bypass by reversibly phosphorylating isocitrate dehydrogenase, ICDH |
721649 |
