EC Number |
Cofactor |
Reference |
---|
5.4.3.8 | more |
during the first half of the reaction pyridoxamine 5'-phosphate is converted to pyridoxal 5'-phosphate, while pyridoxamine 5'-phosphate is regenerated in the second half of the reaction upon 5-aminolevulinate formation |
746660 |
5.4.3.8 | more |
in both the pyridoxamine 5'-phosphate- and pyridoxal 5'-phosphate-bound structures, the gating loops are well-defined in electron density and are in the ordered open conformation. The conformation of the gating loop is symmetrical |
747005 |
5.4.3.8 | pyridoxal 5'-phosphate |
- |
649844, 653764 |
5.4.3.8 | pyridoxal 5'-phosphate |
a pyridoxamine 5'-phosphate (PMP)/pyridoxal 5'-phosphate (PLP)-dependent enzyme, binding structure with a Schiff base linkage between the cofactor and the epsilon-amino group of Lys286, overview |
747005 |
5.4.3.8 | pyridoxal 5'-phosphate |
a pyridoxamine 5'-phosphate (PMP)/pyridoxal 5'-phosphate (PLP)-dependent enzyme, binding structure, overview |
746660 |
5.4.3.8 | pyridoxal 5'-phosphate |
acts as cofactor and stimulates |
3438 |
5.4.3.8 | pyridoxal 5'-phosphate |
cofactor is bound by a Schiff base to the protein |
3435 |
5.4.3.8 | pyridoxal 5'-phosphate |
dependent on |
703619, 714041, 716103 |
5.4.3.8 | pyridoxal 5'-phosphate |
dependent on, during the catalytic cycle, the cofactor undergoes conversion from pyridoxamine 5'-phosphate to pyridoxal 5'-phosphate, conformational changes and binding structures, overview |
727125 |
5.4.3.8 | pyridoxal 5'-phosphate |
pyridoxal 5'-phosphate binding site |
3444 |