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	
1.5.5.2	FAD	proline dehydrogenase from Thermus thermophilus does not discriminate between FAD and FMN as cofactor, redox active prosthetic group	743834	
1.5.5.2	FAD	TcPRODH is a FAD-dependent protein, key residues involved in cofactor (FAD) binding are Arg431 and Glu559	743635	
1.5.5.2	FMN	-	739932	
1.5.5.2	FMN	proline dehydrogenase from Thermus thermophilus does not discriminate between FAD and FMN as cofactor, redox active prosthetic group	743834	
1.5.5.2	additional information	the recombinant holo form of MBP-tagged TtProDH, as produced in Escherichia coli TOP10 cells, contains about three times more FMN than FAD. The crystal structure of TtProDH variant DELTAABC, which lacks helices alphaA, alphaB and alphaC, shows no electron density for an AMP moiety of the cofactor. ProDH adopts a distorted (betalpha)8 TIM-barrel fold and is the only known TIM-barrel enzyme that contains an FAD cofactor. One cofactor molecule per enzyme subunit	743834	
1.5.5.2	phenazine methosulfate	-	742487	
1.5.5.2	[4Fe-4S]-center	-	739932