1.5.5.2	ATP	-	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	cytochrome c	-	743635	
1.5.5.2	FAD	-	392556, 392560, 392570, 696361, 724345, 724389, 739932, 742487	
1.5.5.2	FAD	1.96 mol per mol of enzyme complex	658668	
1.5.5.2	FAD	determination of key amino acids involved in FAD-binding site and catalysis reaction, involving residues Ser165, Lys195 and Ala252	742641	
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	
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	flavin cofactor, 1.2fold stimulated by exogenous FAD	722591	
1.5.5.2	FAD	non-covalent binding	741732