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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Subunits
Subunits on EC 1.1.1.82 - malate dehydrogenase (NADP+)
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dimer
monomer
tetramer
additional information
?
Sorghum sp.
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x * 40000, wild-type enzyme and mutant enzymes C64S, C69S, C64S/C69S, SDS-PAGE
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Sorghum sp.
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x * 33000, DELTAN, a truncation mutant corresponding to the deletion of the 5' end of the mdh cDNA open reading frame until the 73rd codon, SDS-PAGE
dimer
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2 * 42000, wild-type enzyme and mutant enzymes C23A, C28A, C23A/C28A, C23A/C28A/C206A, C23A/C28A/C364A, C23A/C28A/C376A, C23A/C28A/C206A/C364A, C23A/C28A/C206A/C376A and C23A/C28A/C364A/C376A, SDS-PAGE
dimer
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2 * 28400, equilibrium sedimentation of the enzyme denatured by 6 M guanidinium chloride, pH 8, and 30 mM 2-mercaptoethanol
dimer
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2 * 43000, unactivated dark enzyme form and activated light enzyme form, SDS-PAGE
4 * 34000, recombinant enzyme, SDS-PAGE, 4 * 33489, sequence calculation
structure qand sequence comaprsion, overall structure, overview
additional information
homology-based 3D modelling of enzyme evidences close positioning of two new disulfide bridges in an accessible region of the protein surface
additional information
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oligomeric states of MDHs, overview
additional information
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enzyme can be interconverted between monomer, dimer and tetramer by varying pH and ionic strength
additional information
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enzyme exists as monomer dimer and tetramer. At neutral pH, pH 7.0-8.6, the enzyme is tetrameric
additional information
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the N-terminal region is located at the surface of the protein. The integrity of the dimeric enzyme is maintained through an N-terminal sequence