1.1.1.39	(S)-malate	above 10 mM	200	
1.1.1.39	(S)-malate	isozyme NAD-ME2, competitive	200	
1.1.1.39	2-Ketoglutarate	-	5098	
1.1.1.39	5'-AMP	isozyme NAD-ME2, competitive versus NAD+, mixed inhibition versus (S)-malate	236	
1.1.1.39	acetyl-CoA	potent inhibitor	29	
1.1.1.39	acetyl-CoA	enzyme activity is allosterically regulated by acetyl-CoA, almost complete inhibition at 0.05 mM	29	
1.1.1.39	acetyl-CoA	-	29	
1.1.1.39	AMP	-	30	
1.1.1.39	ATP	competitive with respect to (S)-malate	4	
1.1.1.39	ATP	-	4	
1.1.1.39	ATP	the enzyme is competitively inhibited by ATP up to 10fold. Addition of 1 mM or 5 mM fumarate reverses ATP-dependent inhibition of the enzyme to 55 or 70% of its maximum activity, respectively	4	
1.1.1.39	bicarbonate	-	1136	
1.1.1.39	Bromopyruvate	-	1917	
1.1.1.39	Ca2+	inhibits 30% at 1 mM and 60% at 10 mM	15	
1.1.1.39	citrate	competitive	131	
1.1.1.39	Cl-	-	141	
1.1.1.39	CO2	chimeric mutant NAD-ME1q, mixed inhibition versus NAD+ and (S)-malate; isozyme NAD-ME2 and chimeric mutant NAD-ME1q, mixed inhibition versus NAD+ and (S)-malate	28	
1.1.1.39	CoA	-	18	
1.1.1.39	CuSO4	-	263	
1.1.1.39	D-Tartrate	-	7181	
1.1.1.39	DL-isocitrate	-	849	
1.1.1.39	DL-lactate	-	5286	
1.1.1.39	EDTA	-	21	
1.1.1.39	EDTA	complete inhibition at 0.1 mM	21	
1.1.1.39	fructose 6-phosphate	competitive versus (S)-malate, 70% inhibition at 2.5 mM	453	
1.1.1.39	fumarate	-	170	
1.1.1.39	glyoxylate	-	101	
1.1.1.39	HCO3-	-	195	
1.1.1.39	HgCl2	-	110	
1.1.1.39	hydroquinone	-	442	
1.1.1.39	KCNO	-	20906	
1.1.1.39	L-asparatate	-	49150	
1.1.1.39	L-aspartate	slightly competitive to malate, only slight inhibition below pH 6.0	97	
1.1.1.39	Li+	slight inhibition	152	
1.1.1.39	Lu3+	strong inhibition, reversible slow-binding mechanism, reversible structural interconversion to the Mn2+-binding form, metal binding site structure	34563	
1.1.1.39	malonate	-	392	
1.1.1.39	Mn2+	inhibits the reductive carboxylation reaction, inhibitory effect is about 20fold reduced by binding of fumarate and L-malate	11	
1.1.1.39	additional information	water stress reduces the enzyme activity in vivo	2	
1.1.1.39	additional information	product inhibition patterns of isozyme NAD-ME2, overview; product inhibition patterns of isozyme NAD-ME2, overview	2	
1.1.1.39	additional information	keeping plants in CO2-free air suppresses the activities of NAD-ME	2	
1.1.1.39	Na+	complete inhibition at 10 mM, no effect by Na+ at 1 mM	59	
1.1.1.39	NADH	-	8	
1.1.1.39	NADH	product inhibition	8	
1.1.1.39	NADH	isozyme NAD-ME2, competitive versus NAD+, mixed inhibition versus (S)-malate. NADH shows competitive and mixed-type inhibition versus NAD+ and (S)-malate with chimeric mutant NAD-ME1q; NADH shows competitive and mixed-type inhibition versus NAD+ and (S)-malate with chimeric mutant NAD-ME1q	8	
1.1.1.39	NEM	-	89	
1.1.1.39	oxalate	-	185	
1.1.1.39	oxalate	very tight binding inhibitor of the NAD-malic enzyme	185	
1.1.1.39	oxaloacetate	-	57	
1.1.1.39	oxaloacetate	competitive versus (S)-malate, 20% inhibition at 2.5 mM	57	
1.1.1.39	PCMB	-	78	
1.1.1.39	phosphoenolpyruvate	-	51	
1.1.1.39	phosphoenolpyruvate	activates at low concentrations, deactivation at high concentrations	51	
1.1.1.39	pyruvate	-	31	
1.1.1.39	pyruvate	product inhibition	31	
1.1.1.39	pyruvate	isozyme NAD-ME2, uncompetitive versus NAD+, mixed inhibition versus (S)-malate. Pyruvate inhibition is uncompetitive with respect to NAD+ and mixed with respect to (S)-malate for the chimeric mutant NAD-ME1q; pyruvate inhibition is uncompetitive with respect to NAD+ and mixed with respect to (S)-malate for the chimeric mutant NAD-ME1q	31	
1.1.1.39	Tartrate	-	762	
1.1.1.39	Tartrate	substrate analogue, isozyme NAD-ME2, uncompetitive versus NAD+, competitive versus (S)-malate	762	
1.1.1.39	Tartronate	-	4283	
1.1.1.39	Tartronate	binding site structure at the active site, competitive	4283	
1.1.1.39	Urea	denaturation, in 3-5 M urea, the enzyme undergoes a reversible tetramer-dimer-monomer quaternary structural change in an acidic pH environment, which resulted in a molten globule state that is prone to aggregate, Mn2+ protects, overview	116