EC Number |
Cofactor |
Reference |
---|
4.2.1.115 | more |
the dehydratase does not require the addition of exogenous cofactor NAD(P)+ |
692984 |
4.2.1.115 | more |
the hexose ring occupies a non-catalytic conformation with respect to the coenzyme |
729735 |
4.2.1.115 | NAD(P)+ |
dependent on, tightly bound |
691202 |
4.2.1.115 | NAD+ |
- |
692952, 694211 |
4.2.1.115 | NADP+ |
binding and binding site structure, overview. Function of Tyr164 is related to its bulkiness in the relay mechanism |
729735 |
4.2.1.115 | NADP+ |
NADP+/NADPH is tightly bound to FlaA1 |
692980 |
4.2.1.115 | NADPH |
binding and binding site structure, overview. Function of Tyr164 is related to its bulkiness in the relay mechanism |
729735 |
4.2.1.115 | NADPH |
superposition of the NADPH binding domain of Mg534 with CapE highlights a large conformational change of the substrate binding domain that reflects the dynamic of the structure during the catalysis. In absence of the substrate, the domain is rotated and closes the substrate binding pocket |
748176 |