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Information on EC 1.1.1.82 - malate dehydrogenase (NADP+)
for references in articles please use BRENDA:EC1.1.1.82
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EC Tree 1 Oxidoreductases
1.1 Acting on the CH-OH group of donors
1.1.1 With NAD+ or NADP+ as acceptor
1.1.1.82 malate dehydrogenase (NADP+)
IUBMB Comments
Activated by light.
The expected taxonomic range for this enzyme is: Eukaryota, Archaea, Bacteria
- 1.1.1.82
- chloroplast
-
nadp-malate
- dikinase
-
3.1.3.11
-
ferredoxin-thioredoxin
- agriculture
showSynonyms
nadp malate dehydrogenase, nadp-linked malate dehydrogenase, malate nadp dehydrogenase, malate dehydrogenase (nadp+), more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
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-malate dehydrogenase
-
-
-
-
NADP-MDH
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(S)-malate + NADP+ = oxaloacetate + NADPH + H+
-
-
-
-
(S)-malate + NADP+ = oxaloacetate + NADPH + H+
The enzyme is highly conserved with plant counterparts, but bearing differences at regulatory determinants with a critical role for redox control of protein activity
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
KEGG
MetaCyc
C4 photosynthetic carbon assimilation cycle, NADP-ME type, C4 photosynthetic carbon assimilation cycle, PEPCK type
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SYSTEMATIC NAME
IUBMB Comments
(S)-malate:NADP+ oxidoreductase
Activated by light.
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CAS REGISTRY NUMBER
COMMENTARY
37250-19-4
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(2S,3R)-tartrate + NAD(P)+
? + NAD(P)H + H+
Substrates: -
Products: -
Products: -
?
(2S,3S)-tartrate + NAD(P)+
? + NAD(P)H + H+
Substrates: -
Products: -
Products: -
?
(S)-malate + NAD(P)+
oxaloacetate + NAD(P)H + H+
Substrates: -
Products: -
Products: -
?
(S)-malate + NADP+
oxaloacetate + NADPH + H+
Substrates: -
Products: -
Products: -
?
(S)-malate + NADP+
oxaloacetate + NADPH + H+
Substrates: -
Products: -
Products: -
?
(S)-malate + NADP+
oxaloacetate + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
(S)-malate + NADP+
oxaloacetate + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
(S)-malate + NADP+
oxaloacetate + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
(S)-malate + NADP+
oxaloacetate + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
(S)-malate + NADP+
oxaloacetate + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
(S)-malate + NADP+
oxaloacetate + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
(S)-malate + NADP+
oxaloacetate + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
(S)-malate + NADP+
oxaloacetate + NADPH + H+
-
Substrates: at pH 8.9 the rate in the direction of NADH oxidation is about 30times that for the reverse direction
Products: -
Products: -
r
oxaloacetate + NADH
(S)-malate + NAD+
-
Substrates: activity with NADPH is about 2.5times that with NADH
Products: -
Products: -
?
oxaloacetate + NADH
(S)-malate + NAD+
-
Substrates: utilization of NADH to NADPH in reduction of oxaloacetate is 1:160
Products: -
Products: -
?
oxaloacetate + NADPH
(S)-malate + NADP+
-
Substrates: under physiological conditions the enzyme functions in the direction of malate formation. Enzyme probably functions in providing the cytoplasm with reducing equivalents in the form of malate which in addition to its various roles, can be used for generation of carbon skeletons for amino acid biosynthesis
Products: -
Products: -
?
oxaloacetate + NADPH
(S)-malate + NADP+
-
Substrates: the enzyme contributes to malate formation during the operation of the C4-dicarboxylic acid pathway of photosynthesis, it possibly also has a photosynthetic function in Calvin cycle plants
Products: -
Products: -
?
oxaloacetate + NADPH
(S)-malate + NADP+
-
Substrates: -
Products: -
Products: -
?
oxaloacetate + NADPH
(S)-malate + NADP+
-
Substrates: enzyme functions in C4 pathway of photosynthesis
Products: -
Products: -
?
oxaloacetate + NADPH
(S)-malate + NADP+
-
Substrates: enzyme may have a common role in both Calvin cycle and C4-photosynthesis
Products: -
Products: -
?
oxaloacetate + NADPH
(S)-malate + NADP+
-
Substrates: -
Products: -
Products: -
?
oxaloacetate + NADPH
(S)-malate + NADP+
-
Substrates: the enzyme contributes to malate formation during the operation of the C4-dicarboxylic acid pathway of photosynthesis, it possibly also has a photosynthetic function in Calvin cycle plants
Products: -
Products: -
?
oxaloacetate + NADPH
(S)-malate + NADP+
-
Substrates: the enzyme contributes to malate formation during the operation of the C4-dicarboxylic acid pathway of photosynthesis, it possibly also has a photosynthetic function in Calvin cycle plants
Products: -
Products: -
?
oxaloacetate + NADPH
(S)-malate + NADP+
-
Substrates: -
Products: -
Products: -
?
oxaloacetate + NADPH
(S)-malate + NADP+
-
Substrates: important enzyme of photosynthetic CO2 fixation
Products: -
Products: -
?
oxaloacetate + NADPH
(S)-malate + NADP+
-
Substrates: key enzyme of the photosynthetic pathway of C4 plants
Products: -
Products: -
?
oxaloacetate + NADPH
(S)-malate + NADP+
Sorghum sp.
-
Substrates: -
Products: -
Products: -
?
oxaloacetate + NADPH
(S)-malate + NADP+
-
Substrates: -
Products: -
Products: -
?
oxaloacetate + NADPH
(S)-malate + NADP+
-
Substrates: the enzyme contributes to malate formation during the operation of the C4-dicarboxylic acid pathway of photosynthesis, it possibly also has a photosynthetic function in Calvin cycle plants
Products: -
Products: -
?
oxaloacetate + NADPH
(S)-malate + NADP+
-
Substrates: enzyme may have a common role in both Calvin cycle and C4-photosynthesis
Products: -
Products: -
?
oxaloacetate + NADPH
(S)-malate + NADP+
-
Substrates: when no reoxidation of the light-generated NADPH can take place because of a lack of electron acceptors, full activation of the enzyme as well as reduction of thioredioxin m is observed. The fine regulation of the reductive activation of the enzyme determines the actual extent of export of reducing equivalents, in the form of malate, via the dicarboxylic acid translocator
Products: -
Products: -
?
oxaloacetate + NADPH
(S)-malate + NADP+
-
Substrates: -
Products: -
Products: -
?
oxaloacetate + NADPH
(S)-malate + NADP+
-
Substrates: at pH 8.9 the rate in the direction of NADH oxidation is about 30times that for the reverse direction
Products: -
Products: -
r
oxaloacetate + NADPH
(S)-malate + NADP+
-
Substrates: the enzyme contributes to malate formation during the operation of the C4-dicarboxylic acid pathway of photosynthesis, it possibly also has a photosynthetic function in Calvin cycle plants
Products: -
Products: -
?
oxaloacetate + NADPH
(S)-malate + NADP+
-
Substrates: key enzyme of the photosynthetic pathway of C4 plants
Products: -
Products: -
?
oxaloacetate + NADPH + H+
(S)-malate + NADP+
Substrates: -
Products: -
Products: -
r
oxaloacetate + NADPH + H+
(S)-malate + NADP+
Substrates: -
Products: -
Products: -
r
oxaloacetate + NADPH + H+
(S)-malate + NADP+
-
Substrates: -
Products: -
Products: -
r
oxaloacetate + NADPH + H+
(S)-malate + NADP+
Substrates: -
Products: -
Products: -
?
oxaloacetate + NADPH + H+
(S)-malate + NADP+
Substrates: -
Products: -
Products: -
?
oxaloacetate + NADPH + H+
(S)-malate + NADP+
Substrates: -
Products: -
Products: -
?
oxaloacetate + NADPH + H+
(S)-malate + NADP+
Substrates: -
Products: -
Products: -
?
oxaloacetate + NADPH + H+
(S)-malate + NADP+
Substrates: -
Products: -
Products: -
?
oxaloacetate + NADPH + H+
(S)-malate + NADP+
Substrates: -
Products: -
Products: -
?
oxaloacetate + NADPH + H+
(S)-malate + NADP+
Substrates: -
Products: -
Products: -
?
oxaloacetate + NADPH + H+
(S)-malate + NADP+
Substrates: -
Products: -
Products: -
?
oxaloacetate + NADPH + H+
(S)-malate + NADP+
-
Substrates: -
Products: -
Products: -
r
oxaloacetate + NADPH + H+
(S)-malate + NADP+
-
Substrates: -
Products: -
Products: -
r
oxaloacetate + NADPH + H+
(S)-malate + NADP+
Substrates: -
Products: -
Products: -
?
oxaloacetate + NADPH + H+
(S)-malate + NADP+
Substrates: -
Products: -
Products: -
?
oxaloacetate + NADPH + H+
(S)-malate + NADP+
Substrates: -
Products: -
Products: -
?
oxaloacetate + NADPH + H+
(S)-malate + NADP+
-
Substrates: -
Products: -
Products: -
r
oxaloacetate + NADPH + H+
(S)-malate + NADP+
Substrates: -
Products: -
Products: -
?
oxaloacetate + NADPH + H+
(S)-malate + NADP+
Substrates: -
Products: -
Products: -
?
oxaloacetate + NADPH + H+
(S)-malate + NADP+
Substrates: -
Products: -
Products: -
?
oxaloacetate + NADPH + H+
(S)-malate + NADP+
Substrates: -
Products: -
Products: -
?
oxaloacetate + NADPH + H+
(S)-malate + NADP+
Substrates: -
Products: -
Products: -
?
oxaloacetate + NADPH + H+
(S)-malate + NADP+
Substrates: -
Products: -
Products: -
?
oxaloacetate + NADPH + H+
(S)-malate + NADP+
Substrates: -
Products: -
Products: -
?
oxaloacetate + NADPH + H+
(S)-malate + NADP+
-
Substrates: -
Products: -
Products: -
r
oxaloacetate + NADPH + H+
(S)-malate + NADP+
-
Substrates: -
Products: -
Products: -
r
additional information
?
-
-
Substrates: the preferential use of NADPH as the cofactor is due to the presence of glycine at position 33
Products: -
Products: -
?
additional information
?
-
Substrates: NADPH is oxidized and oxalacetate is reduced to malate by NADP-MDH
Products: -
Products: -
?
additional information
?
-
Substrates: NADPH is oxidized and oxalacetate is reduced to malate by NADP-MDH
Products: -
Products: -
?
additional information
?
-
-
Substrates: the preferential use of NADPH as the cofactor is due to the presence of glycine at position 33
Products: -
Products: -
?
additional information
?
-
-
Substrates: the preferential use of NADPH as the cofactor is due to the presence of glycine at position 33
Products: -
Products: -
?
additional information
?
-
-
Substrates: the dual specificity for the cofactor results from alanine at position 53 in Methanobacterium jannaschii
Products: -
Products: -
?
additional information
?
-
-
Substrates: the preferential use of NADPH as the cofactor is due to the presence of glycine at position 33
Products: -
Products: -
?
additional information
?
-
-
Substrates: the preferential use of NADPH as the cofactor is due to the presence of glycine at position 33
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(S)-malate + NADP+
oxaloacetate + NADPH + H+
Substrates: -
Products: -
Products: -
?
(S)-malate + NADP+
oxaloacetate + NADPH + H+
Substrates: -
Products: -
Products: -
?
(S)-malate + NADP+
oxaloacetate + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
(S)-malate + NADP+
oxaloacetate + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
(S)-malate + NADP+
oxaloacetate + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
(S)-malate + NADP+
oxaloacetate + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
(S)-malate + NADP+
oxaloacetate + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
(S)-malate + NADP+
oxaloacetate + NADPH + H+
-
Substrates: -
Products: -
Products: -
r
oxaloacetate + NADPH
(S)-malate + NADP+
-
Substrates: under physiological conditions the enzyme functions in the direction of malate formation. Enzyme probably functions in providing the cytoplasm with reducing equivalents in the form of malate which in addition to its various roles, can be used for generation of carbon skeletons for amino acid biosynthesis
Products: -
Products: -
?
oxaloacetate + NADPH
(S)-malate + NADP+
-
Substrates: the enzyme contributes to malate formation during the operation of the C4-dicarboxylic acid pathway of photosynthesis, it possibly also has a photosynthetic function in Calvin cycle plants
Products: -
Products: -
?
oxaloacetate + NADPH
(S)-malate + NADP+
-
Substrates: enzyme functions in C4 pathway of photosynthesis
Products: -
Products: -
?
oxaloacetate + NADPH
(S)-malate + NADP+
-
Substrates: enzyme may have a common role in both Calvin cycle and C4-photosynthesis
Products: -
Products: -
?
oxaloacetate + NADPH
(S)-malate + NADP+
-
Substrates: the enzyme contributes to malate formation during the operation of the C4-dicarboxylic acid pathway of photosynthesis, it possibly also has a photosynthetic function in Calvin cycle plants
Products: -
Products: -
?
oxaloacetate + NADPH
(S)-malate + NADP+
-
Substrates: the enzyme contributes to malate formation during the operation of the C4-dicarboxylic acid pathway of photosynthesis, it possibly also has a photosynthetic function in Calvin cycle plants
Products: -
Products: -
?
oxaloacetate + NADPH
(S)-malate + NADP+
-
Substrates: important enzyme of photosynthetic CO2 fixation
Products: -
Products: -
?
oxaloacetate + NADPH
(S)-malate + NADP+
-
Substrates: key enzyme of the photosynthetic pathway of C4 plants
Products: -
Products: -
?
oxaloacetate + NADPH
(S)-malate + NADP+
-
Substrates: the enzyme contributes to malate formation during the operation of the C4-dicarboxylic acid pathway of photosynthesis, it possibly also has a photosynthetic function in Calvin cycle plants
Products: -
Products: -
?
oxaloacetate + NADPH
(S)-malate + NADP+
-
Substrates: enzyme may have a common role in both Calvin cycle and C4-photosynthesis
Products: -
Products: -
?
oxaloacetate + NADPH
(S)-malate + NADP+
-
Substrates: when no reoxidation of the light-generated NADPH can take place because of a lack of electron acceptors, full activation of the enzyme as well as reduction of thioredioxin m is observed. The fine regulation of the reductive activation of the enzyme determines the actual extent of export of reducing equivalents, in the form of malate, via the dicarboxylic acid translocator
Products: -
Products: -
?
oxaloacetate + NADPH
(S)-malate + NADP+
-
Substrates: the enzyme contributes to malate formation during the operation of the C4-dicarboxylic acid pathway of photosynthesis, it possibly also has a photosynthetic function in Calvin cycle plants
Products: -
Products: -
?
oxaloacetate + NADPH
(S)-malate + NADP+
-
Substrates: key enzyme of the photosynthetic pathway of C4 plants
Products: -
Products: -
?
oxaloacetate + NADPH + H+
(S)-malate + NADP+
Substrates: -
Products: -
Products: -
r
oxaloacetate + NADPH + H+
(S)-malate + NADP+
Substrates: -
Products: -
Products: -
r
oxaloacetate + NADPH + H+
(S)-malate + NADP+
-
Substrates: -
Products: -
Products: -
r
oxaloacetate + NADPH + H+
(S)-malate + NADP+
-
Substrates: -
Products: -
Products: -
r
oxaloacetate + NADPH + H+
(S)-malate + NADP+
-
Substrates: -
Products: -
Products: -
r
oxaloacetate + NADPH + H+
(S)-malate + NADP+
-
Substrates: -
Products: -
Products: -
r
oxaloacetate + NADPH + H+
(S)-malate + NADP+
-
Substrates: -
Products: -
Products: -
r
oxaloacetate + NADPH + H+
(S)-malate + NADP+
-
Substrates: -
Products: -
Products: -
r
additional information
?
-
Substrates: NADPH is oxidized and oxalacetate is reduced to malate by NADP-MDH
Products: -
Products: -
?
additional information
?
-
Substrates: NADPH is oxidized and oxalacetate is reduced to malate by NADP-MDH
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NAD+
NADP+ is the preferred cofactor compared to NAD+ with substrate (S)-malate, while NAD+ is preferred with substrate tartrate. Ala at position 53 is responsible for coenzyme specificity, and the next residue, Arg, is important for NADP+ binding, structural analysis and comparison
NADP+
NADP+ is the preferred cofactor compared to NAD+ with substrate (S)-malate, while NAD+ is preferred with substrate tartrate. Ala at position 53 is responsible for coenzyme specificity, and the next residue, Arg, is important for NADP+ binding, structural analysis and comparison
NADP+
-
NADP+ binds to Ser9, Arg34, His36, Ser37, Ile121, Asn123, and Glu219
NADPH
-
nicotinamide binds to the hydrophobic cleft of MDH from Thermus flavus composed of Leu40, Ile42, Ile107, Thr9, Gly10, Gly87, and Ala88
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mg2+
-
not essential, stimulates up to 20%, optimal concentration is 10 mM MgCl2
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
diethyldicarbonate
-
inactivation follows pseudo-first-order reaction kinetics, partial protection by NADP+, complete protection in presence of NADP+, 0.25 M hydroxylamine causes total reversal of inhibition
HgCl2
-
activity of the oxidized enzyme in presence of guanidine is unaffected by 0.1 mM HgCl2 in presence of 1 mM EDTA and by 0.005 mM HgCl2 in absence of EDTA, activity of the reduced form of enzyme is completely abolished
NADPH
-
MDH activity is inhibited by over 200 mM NADPH
NEM
-
1 mM, activity of the oxidized enzyme in presence of guanidine is unaffected, activity of the reduced form of enzyme is completely abolished