1.1.1.387	2-aminomalonate semialdehyde	spontaneous	Pyrobaculum calidifontis	2-aminoacetaldehyde + CO2	-	?	460483	
1.1.1.387	3-hydroxypropionate + NAD+	-	Pyrobaculum calidifontis	? + NADH + H+	-	?	460599	
1.1.1.387	D-glycerate + NAD+	-	Pseudomonas aeruginosa	?	-	?	431759	
1.1.1.387	D-serine + NAD+	overall reaction, 5% of the relative activity observed with L-serine	Pyrobaculum calidifontis	2-aminoacetaldehyde + CO2 + NADH + H+	-	?	460978	
1.1.1.387	DL-3-hydroxyisobutyrate + NAD+	-	Pyrobaculum calidifontis	? + NADH + H+	-	?	461015	
1.1.1.387	DL-glycerate + NAD+	-	Pyrobaculum calidifontis	? + NADH + H+	-	?	461016	
1.1.1.387	DL-threonine + NAD+	-	Pseudomonas aeruginosa	?	-	?	431818	
1.1.1.387	L-serine + NAD(P)+	-	Pyrobaculum calidifontis	2-aminomalonate semialdehyde + NAD(P)H + H+	-	?	461180	
1.1.1.387	L-serine + NAD+	the enzyme might be involved in serine/threonine degradation. Since growth experiments with various nitrogen and carbon sources (including L-serine) reveal no difference between the Pseudomonas aeruginosa wild-type and PA0743 deletion strains, it is suggested hat this organism might contain other (complementing) serine dehydrogenases	Pseudomonas aeruginosa	?	-	?	188041	
1.1.1.387	L-serine + NAD+	the enzyme might be involved in serine/methylserine degradation. Since growth experiments with various nitrogen and carbon sources (including L-serine) reveal no difference between the Pseudomonas aeruginosa wild-type and PA0743 deletion strains, it is suggested hat this organism might contain other (complementing) serine dehydrogenases	Pseudomonas aeruginosa	?	-	?	188041	
1.1.1.387	L-serine + NAD+	overall reaction, NAD+ is the preferred cofactor	Pyrobaculum calidifontis	2-aminoacetaldehyde + CO2 + NADH + H+	-	?	461182	
1.1.1.387	L-serine + NADP+	overall reaction, low activity with NADP+	Pyrobaculum calidifontis	2-aminoacetaldehyde + CO2 + NADPH + H+	-	?	461183	
1.1.1.387	methyl 2,2-dimethyl-3-hydroxypropionate + NAD+	-	Pseudomonas aeruginosa	?	-	?	432121	
1.1.1.387	additional information	modeling of the D-serine and 3-hydroxypropionate molecules into the enzyme's active site. No steric hindrance is observed between D-serine and the side chains of the active site residues. D-serine is placed at the position through interactions similar to the L-serine binding model. The C3 hydrogen of D-serine is located at the same position as that of L-serine. This may explain the high reactivity toward D-serine exhibited by Pyrobaculum calidifontis L-SerDH	Pyrobaculum calidifontis	?	-	-	89