3.5.4.6	additional information	-	additional information	-	209681, 209682, 209686, 209689, 209690, 209691, 209693, 209694	
3.5.4.6	additional information	-	additional information	at pH 7.0 the reaction catalysed by AMP-deaminase from human preterm placenta follows a well depicted sigmoid-shaped kinetic profile, with a half-saturation constant (S0.5) value of about 9.2 mM. Phosphate hardly influences the kinetic profile diminishing the S0.5 constant value slightly to 8.1 mM. Addition into the medium of 1 mM adenine nucleotide, ADP or ATP, transforms the sigmoid-shaped profile of the control kinetic curve into a hyperbolic one, diminishing simultaneously the value of the S0.5 constant from 9.2 mM to 2.4 mM, respectively. Kinetic analysis, overview	720641	
3.5.4.6	additional information	-	additional information	kinetics	654807	
3.5.4.6	additional information	-	additional information	kinetics, stearyl-CoA influences the reaction kinetics	656779	
3.5.4.6	0.223	-	AMP	pH 6.0, 40°C	756756	
3.5.4.6	0.27	-	AMP	pH 6.0, temperature not specified in the publication	755821	
3.5.4.6	0.4	-	AMP	crude enzyme extract, pH 6.5, 20°C	654859	
3.5.4.6	0.54	-	AMP	-	209712	
3.5.4.6	0.6	-	AMP	-	209713	
3.5.4.6	0.6	-	AMP	imidazole-eluted purified enzyme, pH 6.5, 20°C	654859