1.4.4.2	2-mercaptoethanol	thiol compound required for maximal activity on glycine-CO2 exchange reaction	391989	
1.4.4.2	dithiothreitol	P and H protein alone jointly catalyze the glycine-CO2 exchange reaction in presence of pyridoxal phosphate and dithiothreitol	391979	
1.4.4.2	dithiothreitol	thiol compound required for maximal activity on glycine-CO2 exchange reaction	391989	
1.4.4.2	GSH	thiol compound required for maximal activity on glycine-CO2 exchange reaction	391989	
1.4.4.2	H-protein	upon addition of exogenous unlipoylated H-protein, kcat increases 190fold, in the absence of the lipoic acid moiety on H-protein, the methylamine adduct with pyridoxal 5'-phosphate (aminomethyl-quinonoid intermediate) is released as the product of the GLDC-catalyzed decarboxylation of glycine	741906	
1.4.4.2	lipoylated H-protein	the presence of the lipoyl moiety on H-protein does not affect the rates of GLDC (or GLDCcoexp)-catalyzed glycine decarboxylation	741906	
1.4.4.2	additional information	the presence of the lipoyl moiety on H-protein does not affect the rates of GLDC (or GLDCcoexp)-catalyzed glycine decarboxylation further corroborates the suggestion that H-protein (or lipoylated H-protein) does not directly participate in and is not required for release of CO2 from glycine in the formation of the pyridoxal 5'-phosphate-quinonoid intermediate, an important distinction that is contrary to earlier findings	741906