6.2.1.4	additional information	-	additional information	kinetic mechanism and thermodynamic parameter values, quasi-steady-state models, evaluation of five different proposed mechanisms, overview. The ordered ter-ter mechanism with dead-end product inhibition of succinate against succinyl-CoA effectively matches kinetic data on pig heart enzyme, thermodynamic-constrained kinetic model	727203	
6.2.1.4	0.004	-	CoA	enzyme form pI 6.4	789	
6.2.1.4	0.005	-	CoA	enzyme form pI 5.8	789	
6.2.1.4	0.006	-	CoA	enzyme forms pI 6.2 and pI 6.0	789	
6.2.1.4	0.007	-	CoA	enzyme form pI 5.9	789	
6.2.1.4	0.007	-	GDP	pH 8.0, 30°C	651897	
6.2.1.4	0.009	-	GTP	enzyme form pI 6.4	789	
6.2.1.4	0.01	-	GTP	enzyme form 6.0	789	
6.2.1.4	0.011	-	GTP	enzyme forms pI 6.2, pI 5.9 and pI 5.8	789	
6.2.1.4	0.014	-	GTP	refolded enzyme	785	
6.2.1.4	0.027	-	GTP	native enzyme	785	
6.2.1.4	0.036	-	CoA	pH 8.0, 30°C	651897	
6.2.1.4	0.036	-	GTP	pH 8.0, 30°C	651897	
6.2.1.4	0.082	-	GTP	mutant enzyme K46E/K114D/V113L/L227F, at pH 7.4 and 21°C	744369	
6.2.1.4	0.086	-	succinyl-CoA	pH 8.0, 30°C	651897	
6.2.1.4	0.143	-	GTP	mutant enzyme K46E/K114D, at pH 7.4 and 21°C	744369	
6.2.1.4	0.145	-	ATP	wild type enzyme, at pH 7.4 and 21°C	744369	
6.2.1.4	0.23	-	ATP	mutant enzyme K46E/K114D, at pH 7.4 and 21°C	744369	
6.2.1.4	0.265	-	ATP	mutant enzyme V113L/L227F, at pH 7.4 and 21°C	744369	
6.2.1.4	0.39	-	succinate	enzyme form pI 6.4	789	
6.2.1.4	0.43	-	succinate	enzyme forms pI 5.9 and pI 5.8	789	
6.2.1.4	0.45	-	succinate	enzyme form pI 6.0	789	
6.2.1.4	0.49	-	succinate	pH 8.0, 30°C	651897	
6.2.1.4	0.49	-	succinate	wild type enzyme, at pH 7.4 and 21°C	743947	
6.2.1.4	0.63	-	GTP	at pH 8.0 and 37°C	745498	
6.2.1.4	2.26	-	phosphate	pH 8.0, 30°C	651897	
6.2.1.4	5.1	-	succinate	mutant enzyme V330M, at pH 7.4 and 21°C	743947