EC Number   |
Cofactor |
Reference |
|---|
    1.1.5.4 | FAD |
in absence of FAD no reduction of 2,6-dichlorophenol indophenol is observed |
287734 |
| 1.1.5.4 | FAD |
is probably a tightly but non-covalently bound prosthetic group |
287733 |
| 1.1.5.4 | FAD |
Km: 0.0004 mM |
287619 |
| 1.1.5.4 | FAD |
noncovalently bound as a prosthetic group |
722575 |
| 1.1.5.4 | FAD |
the enzyme requires FAD and vitamin K for activity |
287730 |
| 1.1.5.4 | FAD |
triple cofactor requirement for FAD, quinone and phospholipid. The formation of reduced forms of FAD is not detected, but in the presence of both FAD and phospholipid the enzyme catalyzes the reduction of quinone by L-malate at rates equivalent to the rate obtained with 2,6-dichlorophenol-indophenol as terminal acceptor. Km-value for FAD is 0.0004 mM |
696072 |
| 1.1.5.4 | menadione |
triple cofactor requirement for FAD, quinone and phospholipid. Maximum rate when phosphatidylethanolamine is added to the enzyme before the quinone |
696072 |
| 1.1.5.4 | menaquinone |
- |
722575 |
| 1.1.5.4 | more |
no spectral evidence for the presence of a flavin or quinone in the purified enzyme |
287730 |
| 1.1.5.4 | more |
the enzyme is active with 2,6-dichlorophenolindophenol |
723124 |
