1.1.1.82	acetone	increases the activity of the oxidized truncated enzyme form, optimal concentration 15%	287392	
1.1.1.82	carboxypeptidase Y	incubation of the native oxidized enzyme at pH 6.0, 25°C, results in slow activation. A small carboxy-terminal peptide of the native enzyme is accessible to proteolytic degradation followed by activation of the inactive oxidized enzyme. This peptide is involved in the regulation of activity, tetramer formation and thioredoxin binding	287392	
1.1.1.82	dithiothreitol	activates	286653, 287384, 287392, 287393, 287410	
1.1.1.82	dithiothreitol	activation of the inactive oxidized enzyme	287419	
1.1.1.82	DTT	activates enzyme in free extracts	657015	
1.1.1.82	guanidine	can activate oxidized enzyme	287405	
1.1.1.82	light	NADP-MDH is a strictly redox-regulated, light-activated enzyme that is inactive in the dark	741200	
1.1.1.82	methanol	increases the activity of the oxidized truncated enzyme form, optimal concentration 8%	287392	
1.1.1.82	additional information	3,4-dichlorophenyl-1,1-dimethylurea inhibits light activation	287402	
1.1.1.82	additional information	3,4-dichlorophenyl-1,1-dimethylurea, up to 0.033 mM, strongly inhibits light activation	287398	
1.1.1.82	additional information	activation by light	287384, 287391, 287395, 287398, 287399, 287412, 287414, 287419, 287425	
1.1.1.82	additional information	activation by light results from the thioredoxin-mediated reduction of two disulfides, located, respectively, in N- and C-terminal sequence extensions typical of all NADP-dependent light-regulated enzyme forms. The activation is a result of the unobstruction of the active site by acquisition of an additional mobility of the C-terminal 15-residue stretch	287395	
1.1.1.82	additional information	in the absence of photosynthetic electron flow, the chloroplast enzyme exists in its disulfide-containing form which is inactive under physiological conditions. Upon interaction with reduced thioredoxin generated in the light, the active dithiol-containing enzyme is formed	287389	
1.1.1.82	additional information	in vivo activity of the enzyme is controlled by a balance between the light-actuated ferredoxin/thioredoxin system for activation and the dark-dependent, as yet unidentified oxidant required for deactivation	287404	
1.1.1.82	additional information	light effect mediator is a surface-exposed, tighly bound protein existing in the thylakoid membranes	287412	
1.1.1.82	additional information	light-mediated reversible activation	287419	
1.1.1.82	additional information	mechanism of light/dark regulation	287399	
1.1.1.82	additional information	noncyclic electron flow is required for activation of the enzyme	287398	
1.1.1.82	additional information	phlorizin, 0.33-1.7 mM slightly inhibits light activation	287398	
1.1.1.82	additional information	structural basis of light-dependent regulation	287423	
1.1.1.82	additional information	the enzyme is activated by light via a ferredoxin-thioredoxin reduction system which reduces disulfide bridges in the enzyme, structural basis for light activation	287414	
1.1.1.82	additional information	the enzyme is active in the light	657015	
1.1.1.82	additional information	thioredoxin-dependent reduction steps are involved in NADP-dependent malate dehydrogenase light activation	287421	
1.1.1.82	reduced thioredoxin	-	739249	
1.1.1.82	thioredoxin	activated by thiol/disulfide interchange with reduced thioredoxin	287422	
1.1.1.82	thioredoxin	activated by thioredoxin m that is reduced either photochemically with ferredoxin and ferredoxin-thioredoxin reductase or chemically with dithiothreitol	287411	
1.1.1.82	thioredoxin	activates	287425, 287427	
1.1.1.82	thioredoxin	activation of the purified enzyme is strictly dependent on thioredoxin	670586	
1.1.1.82	thioredoxin	enzyme is activated by reduction of its N-terminal and C-terminal disulfides by reduced thioredoxin. The activation is inhibited by NADP+	287424	
1.1.1.82	thioredoxin	immunolocalisation experiments suggest that both thioredoxins (f and m) are involved in activation of NADP-linked malate dehydrogenase in the pea leaf chloroplast	689663	
1.1.1.82	thioredoxin	reduced thioredoxins, TRXs, activate the NADP-dependent malate dehydrogenase	739249	
1.1.1.82	thioredoxin	strong activation	287397	
1.1.1.82	thioredoxin	the N-terminal disulfide formed between C24 and C29 has a more positive oxidation-reduction midpoint potential than the two other disulfides and is thus likely to be the preregulatory disulfide postulated to function in activating the enzyme	287425	
1.1.1.82	thioredoxin	thioredoxin-dependent reduction steps are involved in NADP-dependent malate dehydrogenase light activation	287421	
1.1.1.82	thioredoxin	thioredoxin/enzyme complex is an integral component of the thioredoxin mechanism responsible for the fine-tuning of the enzyme activity, the N-terminal 37 amino residues are involved in providing a specific thioredoxin binding-site	287427