EC Number   |
Cofactor |
Reference |
|---|
   2.6.1.52 | pyridoxal 5'-phosphate |
- |
640150, 640151, 640154, 640157, 640158, 640161, 663339, 721168, 722253, 731270, 759123 |
| 2.6.1.52 | pyridoxal 5'-phosphate |
Km 0.005 mM |
640160 |
| 2.6.1.52 | pyridoxal 5'-phosphate |
PLP |
758704, 758955, 759278, 759344 |
| 2.6.1.52 | pyridoxal 5'-phosphate |
PLP, dependent on |
759886 |
| 2.6.1.52 | pyridoxal 5'-phosphate |
PLP, dependent on, the PLP prosthetic group creates a Schiff base (internal aldimine) between C4' and Nzeta of K265, PLP bound in the active site forms an internal aldimine with residue K265, the residue placed in the coil between beta9 and beta10 |
759284 |
| 2.6.1.52 | pyridoxal 5'-phosphate |
presence of cofactor influences the tertiary structure. The cofactor does not influence the secondary structure of the enzyme. Stability of the protein is significantly affected by the cofactor as holo-enzyme shows higher values for thermal and GdnHCl-induced denaturation, respectively, when compared to the apoenzyme. The cofactor also influences the unfolding pathway of the enzyme. Although urea-dependent unfolding of both holo- and apo-EhPSAT is a three-state process, the intermediates stabilized during unfolding are significantly different. For the holo-enzyme a dimeric holo-intermediate is stabilized, whereas for the apo-enzyme, a monomeric intermediate is stabilized |
722154 |
