1.2.1.90	additional information	-	D-glyceraldehyde 3-phosphate	the saturation with D-glyceraldehyde 3-phosphate follows classical Michaelis-Menten kinetics, showing half-maximal saturation at 50 mM. A definite Km for the free aldehyde, the presumed substrate of the enzyme, cannot be given because the portion of the free aldehyde in aqueous solution could not be determined at 70 °C	727825	
1.2.1.90	0.02	-	D-glyceraldehyde 3-phosphate	pH 7.0, 45°C	727454	
1.2.1.90	0.02	-	D-glyceraldehyde 3-phosphate	pH 7.0, 70°C	727454	
1.2.1.90	0.23	-	NADP+	pH 8.5, 30°C, recombinant enzyme, with succinate semialdehyde	762770	
1.2.1.90	0.4	-	NAD+	pH 8.5, 30°C, recombinant enzyme, with succinate semialdehyde	762770	
1.2.1.90	1	-	NAD+	pH 7.0, 45°C	727454	
1.2.1.90	1.9	-	D-glyceraldehyde 3-phosphate	pH 8.5, 30°C, recombinant enzyme, with NADP+	762770	
1.2.1.90	2.2	-	D-glyceraldehyde 3-phosphate	pH 8.5, 30°C, recombinant enzyme, with NAD+	762770	
1.2.1.90	3	-	L-Glyceraldehyde 3-phosphate	about, pH 8.5, 30°C, recombinant enzyme, with NADP+	762770	
1.2.1.90	3.1	-	NAD+	pH 7.0, 70°C	727454