1.5.5.2	FAD	-	392556, 392560, 392570, 696361, 724345, 724389, 739932, 742487	
1.5.5.2	FAD	FAD may be released by 1 M KBr, apoprotein has no proline dehydrogenase activity but may be restored by external addition of FAD	392571	
1.5.5.2	FAD	1.96 mol per mol of enzyme complex	658668	
1.5.5.2	FAD	flavin cofactor, 1.2fold stimulated by exogenous FAD	722591	
1.5.5.2	ATP	-	739932	
1.5.5.2	FMN	-	739932	
1.5.5.2	[4Fe-4S]-center	-	739932	
1.5.5.2	coenzyme Q1	coenzyme Q1 is electron acceptor for PRODH/POX, which passes electrons directly to coenzyme Q1 (CoQ1) RODH/POX binds directly to CoQ1 without the formation of a tertiary complex. The transfer of electrons from proline to CoQ1 by PRODH/POX is dependent on downstream electron transfer from CoQ1 to Complexes III and IV	741588	
1.5.5.2	FAD	non-covalent binding	741732	
1.5.5.2	FAD	enzyme-bound, dependent on. Addition of excess FAD hardly improves the enzyme activity, confirming that the enzyme is fully saturated with FAD	742162