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	additional information	no spectral evidence for the presence of a flavin or quinone in the purified enzyme	287730	
1.1.5.4	additional information	the enzyme is active with 2,6-dichlorophenolindophenol	723124	
1.1.5.4	additional information	the enzymeis active with duroquinone and dimethyl naphthoquinone	722575	
1.1.5.4	ubiquinone	-	722575, 723124	
1.1.5.4	ubiquinone-0	triple cofactor requirement for FAD, quinone and phospholipid. Maximum activation rate when phosphatidylethanolamine is added to the enzyme before the quinone	696072	
1.1.5.4	ubiquinone-1	the route of electrons in this assay is unclear, but it probably leads from the enzyme either directly or via quinones to 2,6-dichlorophenol indophenol. The malate-dependent 2,6-dichlorophenol indophenol reduction rate catalyzed by Helicobacter pylori membranes could be stimulated by 30 to 50% by the addition of 60 mM ubiquinone-1. This suggests that quinones play, at least in part, an intermediary role in the reduction of the dye	287737	
1.1.5.4	ubiquinone-9	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. The quinone is identified as ubiquinone 9. Km-value for ubiquinone 9 is 0.0024 mM	696072	
1.1.5.4	vitamin K1	the enzyme requires FAD and vitamin K for activity	287730	
1.1.5.4	vitamin K1	with both vitamin K1 and ubiquinone-9, maximum rates are obtained by exposing the enzyme to phospholipid and quinone simultaneously, but, when phosphatidylethanolamine is added to the enzyme before either of these quinones, the rates are much lower	696072