EC Number   |
Cofactor |
Reference |
|---|
   1.14.18.2 | cytochrome b5 |
- |
744458, 745641, 746206, 746215 |
| 1.14.18.2 | ferrocytochrome b5 |
- |
639331, 685822 |
| 1.14.18.2 | ferrocytochrome b5 |
2 electrons are donated by either NADH or NADPH are transported via cytochrome b5 in the CMP-NeuAc hydroxylation system of mouse liver cytosol |
639315 |
| 1.14.18.2 | ferrocytochrome b5 |
binding of CMP-N-acetylneuraminate to CMP-N-acetylneuraminate hydroxylase changes conformation of the enzyme so as to construct a recognition site for cytochrome b5, followed by the formation of a ternary complex through this domain. Then the transport of electrons from NAD(P)H to the enzyme through cytochrome b5 takes place, CMP-N-acetylneuraminate is converted to CMP-N-glycoloylneuraminic acid and finally the ternary complex dissociates into its components to release CMP-N-glycoloylneuraminic acid |
639326 |
| 1.14.18.2 | ferrocytochrome b5 |
evidence for the formation of a ternary complex of hydroxylase, CMP-Neu5Ac and cytochrome b5 |
639332 |
| 1.14.18.2 | ferrocytochrome b5 |
pure hydrophilic cytochrome b5 interacts more effectively with the hydroxylase than isolated amphiphytic cytochrome b5 |
639319 |
| 1.14.18.2 | ferrocytochrome b5 |
the electron carrier cytochrome b5 is essential for activity |
639334 |
| 1.14.18.2 | NADH |
- |
639314, 639319, 639320, 639321, 639327, 639329, 639331, 639332, 639333, 639334 |
| 1.14.18.2 | NADH |
most effective cofactor, optimal activity at 0.4 mM NADH, higher concentrations are slightly inhibitory |
639325 |
| 1.14.18.2 | NADH |
NADH is much more effective than NADPH |
639315 |
