EC Number   |
Activating Compound |
Reference |
|---|
    4.1.1.11 | acetyl-CoA |
acetyl-CoA is required for activation |
726873 |
| 4.1.1.11 | CoA |
NMR spectroscopy demonstrates that CoA is an absolute requirement for PanD-PanZ complex formation, the binding site for AcCoA is very close to the protein-protein interface. PanZ promotes the activation of the zymogen of PanD to form aspartate alpha-decarboxylase (ADC) in a CoA-dependent manner |
747497 |
| 4.1.1.11 | more |
no activation with the CoA-binding-deficient PanMG76L variant |
728234 |
| 4.1.1.11 | more |
role for Thr57 in the activation of the enzyme, while neither Tyr58 nor Tyr22 is required for the activation reaction, overview |
726592 |
| 4.1.1.11 | more |
the enzyme does not require activation by an endogenous PanM-like protein, incontrast to other species like Escherichia coli or Salmonella enterica |
728327 |
| 4.1.1.11 | PanM |
Salmonella enterica PanM, formerly YhhK, a Gcn5-like N-acetyltransferase, is necessary for pro-PanD maturation, both in vitro and in vivo. PanM-dependent pro-PanD maturation does not involve an acetyl transfer event. CoA binding to PanM is needed for in vivo activity, disruption of CoA binding prevents PanM from interacting with PanD. PanM lacks acetyltransferase activity but functions instead as an acetyl-coenzyme A (CoA) sensor, overview |
728234 |
| 4.1.1.11 | PanZ |
analysis of the protein complex between Escherichia coli PanD and PanZ in vitro using isothermal titration calorimetry and mass spectrometry and thereby determine the stoichiometry and affinity of the components of this protein complex, high affinity 4:4 heterooctameric complex, overview. Non-covalent interaction between the acetyl group of acetyl-CoA and the PanD zymogen may be required to induce activation |
726873 |
| 4.1.1.11 | PanZ |
PanD is activated by the putative acetyltransferase YhhK, termed PanZ. Activation of PanD both in vivo and in vitro is PanZ-dependent. PanZ binds to PanD. Gene panZ is conserved only in Escherichia coli-related enterobacterial species including Shigella, Salmonella, Klebsiella and Yersinia |
728266 |
| 4.1.1.11 | PanZ |
structure of the complex of PanD and its activating factor PanZ, overview. Binding of AcCoA to PanZ is required to form the PanZ/PanD interface. PanZ-AcCoA activates PanD via selection of a reactive conformation of PanD. PanZ is essential for activation of the zymogen PanD to form the mature enzyme in vivo, and its deletion leads to beta-alanine auxotrophy. NMR spectroscopy demonstrates that CoA is an absolute requirement for PanD-PanZ complex formation. PanZ inhibits catalytic activity by activated PanD. Structural basis for activation, overview |
747497 |
| 4.1.1.11 | PanZ |
the enzyme requires activation by PanZ to be posttranslationally cleaved |
747593 |
