1.1.1.82: malate dehydrogenase (NADP+)
This is an abbreviated version!
For detailed information about malate dehydrogenase (NADP+), go to the full flat file.
Word Map on EC 1.1.1.82
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1.1.1.82
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chloroplast
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nadp-malate
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dikinase
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3.1.3.11
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ferredoxin-thioredoxin
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agriculture
- 1.1.1.82
- chloroplast
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nadp-malate
- dikinase
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3.1.3.11
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ferredoxin-thioredoxin
- agriculture
Reaction
Synonyms
(S)-malate dehydrogenase, dehydrogenase, malate (nicotinamide adenine dinucleotide phosphate), L-malate:NAD oxidoreductase, malate NADP dehydrogenase, malic dehydrogenase (nicotinamide adenine dinucleotide phosphate), MDH, NADP malate dehydrogenase, NADP+-dependent malate dehydrogenase, NADP-dependent malate dehydrogenase, NADP-linked malate dehydrogenase, NADP-malate dehydrogenase, NADP-malic enzyme, NADP-MDH, NADP-MDH1, NADP-MDH2, NADPH-MDH
ECTree
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Activating Compound
Activating Compound on EC 1.1.1.82 - malate dehydrogenase (NADP+)
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acetone
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increases the activity of the oxidized truncated enzyme form, optimal concentration 15%
carboxypeptidase Y
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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
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light
NADP-MDH is a strictly redox-regulated, light-activated enzyme that is inactive in the dark
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methanol
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increases the activity of the oxidized truncated enzyme form, optimal concentration 8%
reduced thioredoxins, TRXs, activate the NADP-dependent malate dehydrogenase
thioredoxin
activation of the purified enzyme is strictly dependent on thioredoxin
thioredoxin
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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
thioredoxin
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immunolocalisation experiments suggest that both thioredoxins (f and m) are involved in activation of NADP-linked malate dehydrogenase in the pea leaf chloroplast
thioredoxin
Sorghum sp.
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thioredoxin-dependent reduction steps are involved in NADP-dependent malate dehydrogenase light activation
thioredoxin
Sorghum sp.
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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
thioredoxin
Sorghum sp.
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enzyme is activated by reduction of its N-terminal and C-terminal disulfides by reduced thioredoxin. The activation is inhibited by NADP+
thioredoxin
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activated by thioredoxin m that is reduced either photochemically with ferredoxin and ferredoxin-thioredoxin reductase or chemically with dithiothreitol
additional information
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light effect mediator is a surface-exposed, tighly bound protein existing in the thylakoid membranes
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additional information
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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
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additional information
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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
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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
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additional information
Sorghum sp.
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thioredoxin-dependent reduction steps are involved in NADP-dependent malate dehydrogenase light activation
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additional information
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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
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additional information
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3,4-dichlorophenyl-1,1-dimethylurea inhibits light activation
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additional information
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3,4-dichlorophenyl-1,1-dimethylurea, up to 0.033 mM, strongly inhibits light activation
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additional information
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noncyclic electron flow is required for activation of the enzyme
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additional information
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phlorizin, 0.33-1.7 mM slightly inhibits light activation
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