EC Number   |
Cofactor |
Reference |
|---|
    5.4.3.5 | pyridoxal 5'-phosphate |
- |
704658, 727677, 748182 |
| 5.4.3.5 | pyridoxal 5'-phosphate |
covalently bound via a Schiff base (imine) to Lys629 |
727131 |
| 5.4.3.5 | pyridoxal 5'-phosphate |
dependent on |
693191 |
| 5.4.3.5 | pyridoxal 5'-phosphate |
Km value 0.0015 |
652199 |
| 5.4.3.5 | pyridoxal 5'-phosphate |
quantum mechanics/molecular mechanics (QM/MM) studies on the mechanism of action of cofactor pyridoxal 5'-phosphate in ornithine 4,5-aminomutase, overview |
747565 |
| 5.4.3.5 | pyridoxal 5'-phosphate |
required, important role of enzyme residue tyrosine 187, which lies planar to the pyridoxal 5'-phosphate pyridine ring. The substrate forms a covalent Schiff base linkage with the imine nitrogen of the pyridoxal 5'-phosphate cofactor. In particular, Tyr187 forms a Pi-stacking interaction with the pyridine ring of pyridoxal 5'-phosphate, the guanidinium side chain of Arg297 forms a salt bridge with the alpha-carboxylate group of the substrate, and residues His225, His182, Asn226, Glu81, and Ser162 provide additional hydrogen bonding interactions with the substrate and cofactor |
747073 |
| 5.4.3.5 | pyridoxal 5'-phosphate |
required, Km: 0.00036 mM |
2074 |
| 5.4.3.5 | pyridoxal 5'-phosphate |
stabilizes high-energy intermediates for performing challenging 1,2-amino rearrangements between adjacent carbons, binding site structure, overview |
727644 |
| 5.4.3.5 | pyridoxal 5'-phosphate |
the protonation state of the pyridoxal 5'-phosphate cofactor has less of a role in radical-mediated chemistry compared to electrostatic interactions between the substrate and protein. Binding structure analysis and comparison with lysien 5,6-aminomutase, EC 5.4.3.3 |
747193 |
| 5.4.3.5 | vitamin B12 |
- |
661645 |
