EC Number   |
Cofactor |
Reference |
|---|
    2.1.2.1 | 5,10-methylenetetrahydrofolate |
- |
735367, 736084, 736499, 736645, 736646, 736753, 737188, 737212, 737301 |
| 2.1.2.1 | pyridoxal 5'-phosphate |
- |
391984, 441402, 441412, 441413, 441415, 441416, 441417, 441418, 441420, 441422, 441429, 441430, 441431, 441432, 441434, 659754, 686353, 703634, 703674, 703863, 704347, 704756, 705602, 719472, 726831, 735367, 736753, 755894, 755905, 755964, 756058, 756098, 756288, 756477, 756534, 756695, 756705, 756725, 756837, 756948, 757362, 757384, 757905, 758045, 758178, 758412 |
| 2.1.2.1 | pyridoxal 5'-phosphate |
2 mol per mol enzyme |
441409, 441410, 441437 |
| 2.1.2.1 | pyridoxal 5'-phosphate |
dependent on |
659772, 702126, 718557, 718775, 718984, 719472, 719529, 736499, 736645, 736646, 737188, 737301, 755784, 755912 |
| 2.1.2.1 | pyridoxal 5'-phosphate |
dependent on, cofactor binding triggers a rearrangement of the small domain that moves toward the large domain and screens the pyridoxal 5'-phosphate binding site at the solvent side |
737212 |
| 2.1.2.1 | pyridoxal 5'-phosphate |
dependent on, stabilizes the dimeric form of the enzyme |
718984 |
| 2.1.2.1 | pyridoxal 5'-phosphate |
dependent on, the apo enzyme has some enzyme activity in the absence of pyridoxal 5'-phosphate but this activity is only slightly above background and can be due to incomplete removal of pyridoxal 5'-phosphate |
705603 |
| 2.1.2.1 | pyridoxal 5'-phosphate |
dependent on. The binding environment of PLP in human and Plasmodium enzymes is significantly different |
736084 |
| 2.1.2.1 | pyridoxal 5'-phosphate |
dimeric form of some mutant enzymes contains no pyridoxal 5'-phosphate |
657811 |
| 2.1.2.1 | pyridoxal 5'-phosphate |
important role in maintaining the structural integrity of the enzyme by preventing the dissociation of the enzyme into subunits, in addition to its function in catalysis |
441426, 441427, 441428 |
