Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(2S,3R)-tartrate + NAD(P)+
? + NAD(P)H + H+
-
-
-
?
(2S,3S)-tartrate + NAD(P)+
? + NAD(P)H + H+
-
-
-
?
(S)-malate + NAD(P)+
oxaloacetate + NAD(P)H + H+
-
-
-
?
(S)-malate + NAD+
oxaloacetate + NADH + H+
-
-
-
r
(S)-malate + NADP+
oxaloacetate + NADPH + H+
oxaloacetate + NADH
(S)-malate + NAD+
oxaloacetate + NADPH
(S)-malate + NADP+
oxaloacetate + NADPH + H+
(S)-malate + NADP+
additional information
?
-
(S)-malate + NADP+
oxaloacetate + NADPH + H+
-
-
-
-
r
(S)-malate + NADP+
oxaloacetate + NADPH + H+
-
-
-
?
(S)-malate + NADP+
oxaloacetate + NADPH + H+
-
-
-
?
(S)-malate + NADP+
oxaloacetate + NADPH + H+
-
-
-
-
r
(S)-malate + NADP+
oxaloacetate + NADPH + H+
-
-
-
-
r
(S)-malate + NADP+
oxaloacetate + NADPH + H+
-
-
-
-
r
(S)-malate + NADP+
oxaloacetate + NADPH + H+
-
-
-
-
r
(S)-malate + NADP+
oxaloacetate + NADPH + H+
-
-
-
-
r
(S)-malate + NADP+
oxaloacetate + NADPH + H+
-
-
-
-
?
(S)-malate + NADP+
oxaloacetate + NADPH + H+
-
-
-
r
(S)-malate + NADP+
oxaloacetate + NADPH + H+
-
-
-
-
r
(S)-malate + NADP+
oxaloacetate + NADPH + H+
-
-
-
-
r
(S)-malate + NADP+
oxaloacetate + NADPH + H+
Sorghum sp.
-
-
-
-
r
(S)-malate + NADP+
oxaloacetate + NADPH + H+
-
-
-
-
r
(S)-malate + NADP+
oxaloacetate + NADPH + H+
-
-
-
-
r
(S)-malate + NADP+
oxaloacetate + NADPH + H+
-
-
-
r
(S)-malate + NADP+
oxaloacetate + NADPH + H+
-
-
-
r
(S)-malate + NADP+
oxaloacetate + NADPH + H+
-
at pH 8.9 the rate in the direction of NADH oxidation is about 30times that for the reverse direction
-
-
r
oxaloacetate + NADH
(S)-malate + NAD+
-
-
-
r
oxaloacetate + NADH
(S)-malate + NAD+
-
activity with NADPH is about 2.5times that with NADH
-
?
oxaloacetate + NADH
(S)-malate + NAD+
-
utilization of NADH to NADPH in reduction of oxaloacetate is 1:160
-
?
oxaloacetate + NADPH
(S)-malate + NADP+
-
-
-
?
oxaloacetate + NADPH
(S)-malate + NADP+
-
-
-
?
oxaloacetate + NADPH
(S)-malate + NADP+
-
-
-
r
oxaloacetate + NADPH
(S)-malate + NADP+
-
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
-
?
oxaloacetate + NADPH
(S)-malate + NADP+
-
-
-
?
oxaloacetate + NADPH
(S)-malate + NADP+
-
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
-
?
oxaloacetate + NADPH
(S)-malate + NADP+
-
-
-
?
oxaloacetate + NADPH
(S)-malate + NADP+
-
-
-
?
oxaloacetate + NADPH
(S)-malate + NADP+
-
-
-
?
oxaloacetate + NADPH
(S)-malate + NADP+
-
-
-
?
oxaloacetate + NADPH
(S)-malate + NADP+
-
-
-
?
oxaloacetate + NADPH
(S)-malate + NADP+
-
enzyme functions in C4 pathway of photosynthesis
-
?
oxaloacetate + NADPH
(S)-malate + NADP+
-
-
-
?
oxaloacetate + NADPH
(S)-malate + NADP+
-
-
-
?
oxaloacetate + NADPH
(S)-malate + NADP+
-
-
-
?
oxaloacetate + NADPH
(S)-malate + NADP+
-
enzyme may have a common role in both Calvin cycle and C4-photosynthesis
-
?
oxaloacetate + NADPH
(S)-malate + NADP+
-
-
-
?
oxaloacetate + NADPH
(S)-malate + NADP+
-
-
-
?
oxaloacetate + NADPH
(S)-malate + NADP+
-
-
-
?
oxaloacetate + NADPH
(S)-malate + NADP+
-
-
-
?
oxaloacetate + NADPH
(S)-malate + NADP+
-
-
-
?
oxaloacetate + NADPH
(S)-malate + NADP+
-
-
-
?
oxaloacetate + NADPH
(S)-malate + NADP+
-
-
-
?
oxaloacetate + NADPH
(S)-malate + NADP+
-
-
-
?
oxaloacetate + NADPH
(S)-malate + NADP+
-
-
-
?
oxaloacetate + NADPH
(S)-malate + NADP+
-
-
-
?
oxaloacetate + NADPH
(S)-malate + NADP+
-
-
-
?
oxaloacetate + NADPH
(S)-malate + NADP+
-
-
-
r
oxaloacetate + NADPH
(S)-malate + NADP+
-
-
-
r
oxaloacetate + NADPH
(S)-malate + NADP+
-
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
-
?
oxaloacetate + NADPH
(S)-malate + NADP+
-
-
-
?
oxaloacetate + NADPH
(S)-malate + NADP+
-
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
-
?
oxaloacetate + NADPH
(S)-malate + NADP+
-
-
-
?
oxaloacetate + NADPH
(S)-malate + NADP+
-
-
-
?
oxaloacetate + NADPH
(S)-malate + NADP+
-
-
-
?
oxaloacetate + NADPH
(S)-malate + NADP+
-
-
-
?
oxaloacetate + NADPH
(S)-malate + NADP+
-
-
-
?
oxaloacetate + NADPH
(S)-malate + NADP+
-
-
?
oxaloacetate + NADPH
(S)-malate + NADP+
-
important enzyme of photosynthetic CO2 fixation
-
?
oxaloacetate + NADPH
(S)-malate + NADP+
-
key enzyme of the photosynthetic pathway of C4 plants
-
?
oxaloacetate + NADPH
(S)-malate + NADP+
Sorghum sp.
-
-
-
?
oxaloacetate + NADPH
(S)-malate + NADP+
Sorghum sp.
-
-
-
?
oxaloacetate + NADPH
(S)-malate + NADP+
Sorghum sp.
-
-
-
?
oxaloacetate + NADPH
(S)-malate + NADP+
Sorghum sp.
-
-
-
?
oxaloacetate + NADPH
(S)-malate + NADP+
Sorghum sp.
-
-
-
r
oxaloacetate + NADPH
(S)-malate + NADP+
-
-
-
?
oxaloacetate + NADPH
(S)-malate + NADP+
-
-
-
?
oxaloacetate + NADPH
(S)-malate + NADP+
-
-
-
?
oxaloacetate + NADPH
(S)-malate + NADP+
-
-
-
?
oxaloacetate + NADPH
(S)-malate + NADP+
-
-
-
?
oxaloacetate + NADPH
(S)-malate + NADP+
-
-
-
?
oxaloacetate + NADPH
(S)-malate + NADP+
-
-
-
?
oxaloacetate + NADPH
(S)-malate + NADP+
-
-
-
?
oxaloacetate + NADPH
(S)-malate + NADP+
-
-
-
?
oxaloacetate + NADPH
(S)-malate + NADP+
-
-
-
?
oxaloacetate + NADPH
(S)-malate + NADP+
-
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
-
?
oxaloacetate + NADPH
(S)-malate + NADP+
-
enzyme may have a common role in both Calvin cycle and C4-photosynthesis
-
?
oxaloacetate + NADPH
(S)-malate + NADP+
-
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
-
?
oxaloacetate + NADPH
(S)-malate + NADP+
-
-
-
?
oxaloacetate + NADPH
(S)-malate + NADP+
-
-
-
?
oxaloacetate + NADPH
(S)-malate + NADP+
-
-
-
?
oxaloacetate + NADPH
(S)-malate + NADP+
-
-
-
?
oxaloacetate + NADPH
(S)-malate + NADP+
-
-
-
?
oxaloacetate + NADPH
(S)-malate + NADP+
-
-
-
?
oxaloacetate + NADPH
(S)-malate + NADP+
-
-
-
?
oxaloacetate + NADPH
(S)-malate + NADP+
-
-
-
?
oxaloacetate + NADPH
(S)-malate + NADP+
-
-
-
?
oxaloacetate + NADPH
(S)-malate + NADP+
-
-
-
?
oxaloacetate + NADPH
(S)-malate + NADP+
-
-
-
r
oxaloacetate + NADPH
(S)-malate + NADP+
-
at pH 8.9 the rate in the direction of NADH oxidation is about 30times that for the reverse direction
-
r
oxaloacetate + NADPH
(S)-malate + NADP+
-
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
-
?
oxaloacetate + NADPH
(S)-malate + NADP+
-
key enzyme of the photosynthetic pathway of C4 plants
-
?
oxaloacetate + NADPH
(S)-malate + NADP+
-
key enzyme of the photosynthetic pathway of C4 plants
-
?
oxaloacetate + NADPH + H+
(S)-malate + NADP+
-
-
-
-
r
oxaloacetate + NADPH + H+
(S)-malate + NADP+
-
-
-
r
oxaloacetate + NADPH + H+
(S)-malate + NADP+
-
-
-
r
oxaloacetate + NADPH + H+
(S)-malate + NADP+
-
-
-
-
r
oxaloacetate + NADPH + H+
(S)-malate + NADP+
-
-
-
-
r
oxaloacetate + NADPH + H+
(S)-malate + NADP+
-
-
-
?
oxaloacetate + NADPH + H+
(S)-malate + NADP+
-
-
-
?
oxaloacetate + NADPH + H+
(S)-malate + NADP+
-
-
-
?
oxaloacetate + NADPH + H+
(S)-malate + NADP+
-
-
-
?
oxaloacetate + NADPH + H+
(S)-malate + NADP+
-
-
-
?
oxaloacetate + NADPH + H+
(S)-malate + NADP+
-
-
-
?
oxaloacetate + NADPH + H+
(S)-malate + NADP+
-
-
-
?
oxaloacetate + NADPH + H+
(S)-malate + NADP+
-
-
-
?
oxaloacetate + NADPH + H+
(S)-malate + NADP+
-
-
-
-
r
oxaloacetate + NADPH + H+
(S)-malate + NADP+
-
-
-
-
r
oxaloacetate + NADPH + H+
(S)-malate + NADP+
-
-
-
?
oxaloacetate + NADPH + H+
(S)-malate + NADP+
-
-
-
-
?
oxaloacetate + NADPH + H+
(S)-malate + NADP+
-
-
-
?
oxaloacetate + NADPH + H+
(S)-malate + NADP+
-
-
-
?
oxaloacetate + NADPH + H+
(S)-malate + NADP+
-
-
-
-
r
oxaloacetate + NADPH + H+
(S)-malate + NADP+
-
-
-
?
oxaloacetate + NADPH + H+
(S)-malate + NADP+
-
-
-
?
oxaloacetate + NADPH + H+
(S)-malate + NADP+
-
-
-
?
oxaloacetate + NADPH + H+
(S)-malate + NADP+
-
-
-
?
oxaloacetate + NADPH + H+
(S)-malate + NADP+
-
-
-
?
oxaloacetate + NADPH + H+
(S)-malate + NADP+
-
-
-
?
oxaloacetate + NADPH + H+
(S)-malate + NADP+
-
-
-
?
oxaloacetate + NADPH + H+
(S)-malate + NADP+
-
-
-
-
r
oxaloacetate + NADPH + H+
(S)-malate + NADP+
-
-
-
-
r
oxaloacetate + NADPH + H+
(S)-malate + NADP+
-
-
-
?
oxaloacetate + NADPH + H+
(S)-malate + NADP+
-
-
-
r
additional information
?
-
-
the preferential use of NADPH as the cofactor is due to the presence of glycine at position 33
-
-
?
additional information
?
-
NADPH is oxidized and oxalacetate is reduced to malate by NADP-MDH
-
-
?
additional information
?
-
NADPH is oxidized and oxalacetate is reduced to malate by NADP-MDH
-
-
?
additional information
?
-
-
the preferential use of NADPH as the cofactor is due to the presence of glycine at position 33
-
-
?
additional information
?
-
-
the preferential use of NADPH as the cofactor is due to the presence of glycine at position 33
-
-
?
additional information
?
-
-
the dual specificity for the cofactor results from alanine at position 53 in Methanobacterium jannaschii
-
-
?
additional information
?
-
-
the preferential use of NADPH as the cofactor is due to the presence of glycine at position 33
-
-
?
additional information
?
-
-
the preferential use of NADPH as the cofactor is due to the presence of glycine at position 33
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.2 - 5.8
(2S,3R)-tartrate
0.8
NAD+
-
cosubstrate malate
0.83
NADH
-
cosubstrate oxaloacetate
additional information
additional information
-
0.2
(2S,3R)-tartrate
pH 10.0, 50°C, with cofactor NAD+, recombinant enzyme
5.8
(2S,3R)-tartrate
pH 10.0, 50°C, with cofactor NADP+, recombinant enzyme
1.2
(2S,3S)-tartrate
pH 10.0, 50°C, with cofactor NAD+, recombinant enzyme
2 - 3
(2S,3S)-tartrate
pH 10.0, 50°C, with cofactor NADP+, recombinant enzyme
0.00012
(S)-malate
-
pH and temperature not specified in the publication
0.00012
(S)-malate
-
pH and temperature not specified in the publication
0.019
(S)-malate
pH 10.0, 50°C, with cofactor NADP+, recombinant enzyme
0.12
(S)-malate
pH 10.0, 50°C, with cofactor NAD+, recombinant enzyme
0.26
(S)-malate
-
pH and temperature not specified in the publication
0.4
(S)-malate
-
pH and temperature not specified in the publication
5
(S)-malate
Sorghum sp.
-
mutant enzyme D201A
10.2
(S)-malate
Sorghum sp.
-
mutant enzyme D201N
12
(S)-malate
Sorghum sp.
-
wild-type enzyme
29
(S)-malate
-
cosubstrate NAD+
32
(S)-malate
-
cosubstrate NADP+
0.000019
NADP+
-
pH and temperature not specified in the publication
0.000019
NADP+
-
pH and temperature not specified in the publication
0.019
NADP+
-
pH and temperature not specified in the publication
0.023
NADP+
-
pH and temperature not specified in the publication
0.073
NADP+
-
cosubstrate malate
0.13
NADP+
-
pH and temperature not specified in the publication
0.011
NADPH
-
-
0.0114
NADPH
Sorghum sp.
-
mutant enzyme D201N
0.02
NADPH
-
pH and temperature not specified in the publication
0.021
NADPH
-
mutant enzyme C23A/C28A and C23A/C28A/C376A, oxidized form
0.023
NADPH
-
mutant enzyme C23A/C28A/C206A/C364A, oxidized form
0.023
NADPH
Sorghum sp.
-
mutant enzyme D201A
0.024
NADPH
-
mutant enzyme C23A/C28A, reduced form
0.026
NADPH
-
mutant enzyme C23A/C28A/C364A and C23A/C28A/C364A/C376A, oxidized form
0.028
NADPH
-
mutant enzyme C23A/C28A/C206A/C376A, oxidized form
0.028
NADPH
Sorghum sp.
-
mutant enzyme C64S/C69S
0.028
NADPH
-
wild-type enzyme and mutant C28A, reduced enzyme form
0.029
NADPH
Sorghum sp.
-
mutant enzyme C207A/E387Q, oxidized form
0.029
NADPH
-
mutant enzyme lacking the N-terminal 45 residues, reduced form
0.03
NADPH
-
mutant enzyme C23A, reduced form
0.03
NADPH
-
recombinant enzyme cloned from expression vector pJ2PCC1
0.031
NADPH
Sorghum sp.
-
mutant enzyme C29S/C207A/E387Q, oxidized enzyme form
0.033
NADPH
-
mutant enzyme C23A/C28A/C206A, oxidized form and mutant DELTAN lacking the N-terminal 45 residues, reduced form
0.035
NADPH
-
enzyme from intermembrane space
0.035
NADPH
Sorghum sp.
-
mutant enzyme C29S/C207A/DELTAEV, oxidized form
0.036
NADPH
-
mutant enzyme C23A/C28A/C206A, reduced form
0.037
NADPH
Sorghum sp.
-
mutant C69S
0.038
NADPH
Sorghum sp.
-
mutant enzyme C64S
0.039
NADPH
Sorghum sp.
-
mutant enzyme DELTAN
0.039
NADPH
-
reduced native enzyme
0.042
NADPH
Sorghum sp.
-
wild-type enzyme
0.043
NADPH
-
recombinant enzyme cloned from expression vector pJCPCC2
0.044
NADPH
Sorghum sp.
-
mutant enzyme C29S/E387Q, reduced form
0.0446
NADPH
Sorghum sp.
-
wild-type enzyme
0.046
NADPH
Sorghum sp.
-
mutant enzyme C29S/E387Q, reduced form
0.046
NADPH
-
oxidized truncated enzyme
0.047
NADPH
Sorghum sp.
-
mutant enzyme C207A/DELTAEV, oxidized form
0.049
NADPH
Sorghum sp.
-
mutant enzyme C29S/DELTAEV, oxidized form
0.06
NADPH
Sorghum sp.
-
mutant enzyme C207A/DELTAEV, and mutant enzyme C29S/C207S/DELTAEV, reduced forms
0.063
NADPH
Sorghum sp.
-
mutant enzyme C29S/DELTAEV, reduced form
0.066
NADPH
-
enzyme from mitochondrial matrix
0.066
NADPH
Sorghum sp.
-
mutant enzyme C29S/C207A/E387Q, reduced form and mutant enzyme C29S/C207A/DELTAEV, reduced form
0.089
NADPH
-
reduced truncated enzyme
0.095
NADPH
-
reduced enzyme, + 200 mM guanidine
0.115
NADPH
Sorghum sp.
-
mutant enzyme C29S/C207A, reduced form
0.22
NADPH
-
oxidized enzyme, + 250 mM guanidine
0.472
NADPH
-
mutant enzyme lacking the N-terminal 45 residues, oxidized form
0.014
oxaloacetate
-
enzyme from intermembrane space
0.017
oxaloacetate
-
mutant enzyme C23A/C28A/C364A/C376A, oxidized form
0.019
oxaloacetate
-
recombinant enzyme cloned from expression vector pJ2PCC2
0.02
oxaloacetate
-
mutant enzyme C23A, reduced form
0.021
oxaloacetate
-
recombinant enzyme cloned from expression vector pJ2PCC1
0.022
oxaloacetate
Sorghum sp.
-
mutant enzyme DELTAN
0.022
oxaloacetate
-
mutant enzyme C23A/C28A, reduced form
0.024
oxaloacetate
-
mutant enzyme C23A/C28A/C206A/C376A, oxidized form
0.025
oxaloacetate
-
mutant enzyme C23A/C28A/C206A/C364A, oxidized form and mutant DELTAN, lacking the 45 N-terminal residues
0.027
oxaloacetate
-
wild-type enzyme, reduced form and mutant enzyme C23A/C28A/C364A, oxidized form
0.028
oxaloacetate
-
mutant enzyme C23A/C28A/C206A, reduced enzyme form and mutant enzyme C23A/C28A/C376A, oxidized form
0.03
oxaloacetate
-
pH and temperature not specified in the publication
0.037
oxaloacetate
Sorghum sp.
-
mutant enzyme C64S
0.037
oxaloacetate
-
enzyme from mitochondrial matrix
0.04
oxaloacetate
Sorghum sp.
-
wild-type enzyme
0.041
oxaloacetate
Sorghum sp.
-
wild-type enzyme
0.042
oxaloacetate
Sorghum sp.
-
mutant C69S
0.042
oxaloacetate
-
reduced truncated enzyme
0.044
oxaloacetate
Sorghum sp.
-
mutant enzyme C64S/C69S
0.048
oxaloacetate
-
reduced native enzyme
0.05
oxaloacetate
Sorghum sp.
-
mutant enzyme C39S/E387Q, reduced form
0.054
oxaloacetate
Sorghum sp.
-
mutant enzyme C207A/DELTAEV, reduced form
0.056
oxaloacetate
-
cosubstrate NADPH
0.056
oxaloacetate
Sorghum sp.
-
mutant enzyme C29S/E387Q, reduced form
0.061
oxaloacetate
-
cosubstrate NADH
0.07
oxaloacetate
Sorghum sp.
-
mutant enzyme C29S/DELTAEV, reduced form
0.077
oxaloacetate
-
reduced enzyme, + 200 mM guanidine
0.086
oxaloacetate
Sorghum sp.
-
mutant enzyme C29S/C207A/E387Q, reduced form
0.094
oxaloacetate
Sorghum sp.
-
mutant enzyme C29S/C207A, reduced form
0.105
oxaloacetate
-
mutant enzyme C23A/C28A/C206A, oxidized form
0.32
oxaloacetate
-
oxidized enzyme, + 250 mM guanidine
0.447
oxaloacetate
Sorghum sp.
-
mutant enzyme C207A/DELTAEV, oxidized form
0.578
oxaloacetate
Sorghum sp.
-
mutant enzyme C29S/DELTAEV, oxidized form
0.583
oxaloacetate
Sorghum sp.
-
mutant enzyme C29S/E387Q, oxidized form
0.894
oxaloacetate
Sorghum sp.
-
mutant enzyme C29S/C207A/E387Q, oxidized form
0.931
oxaloacetate
Sorghum sp.
-
mutant enzyme C29S/C207A/DELTAEV, oxidized form
1.2
oxaloacetate
-
oxidized truncated enzyme
1.8
oxaloacetate
Sorghum sp.
-
mutant enzyme D201N
3
oxaloacetate
Sorghum sp.
-
mutant enzyme D201A
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
evolution
-
MDH is a ubiquitous enzyme found in prokaryotic and eukaryotic organisms. The enzyme belongs to the superfamily of 2-ketoacid NAD(P)+-dependent dehydrogenases. MDH has diverged into two distinct phylogenetic groups. One group includes cytoplasmic MDH, chloroplast MDH, and MDH from Thermus flavus, the other group includes MDHs that are similar to lactate dehydrogenase (LDH). Structure comparisons, the MDHs are mostly dimeric or tetrameric, overview
evolution
-
MDH is a ubiquitous enzyme found in prokaryotic and eukaryotic organisms. The enzyme belongs to the superfamily of 2-ketoacid NAD(P)+-dependent dehydrogenases. MDH has diverged into two distinct phylogenetic groups. One group includes cytoplasmic MDH, chloroplast MDH, and MDH from Thermus flavus; the other group includes MDHs that are similar to lactate dehydrogenase (LDH)
evolution
-
MDH is a ubiquitous enzyme found in prokaryotic and eukaryotic organisms. The enzyme belongs to the superfamily of 2-ketoacid NAD(P)+-dependent dehydrogenases. MDH has diverged into two distinct phylogenetic groups. One group includes cytoplasmic MDH, chloroplast MDH, and MDH from Thermus flavus; the other group includes MDHs that are similar to lactate dehydrogenase (LDH). Structure comparisons, the MDHs are mostly dimeric or tetrameric, overview
evolution
-
MDH is a ubiquitous enzyme found in prokaryotic and eukaryotic organisms. The enzyme belongs to the superfamily of 2-ketoacid NAD(P)+-dependent dehydrogenases. MDH has diverged into two distinct phylogenetic groups. One group includes cytoplasmic MDH, chloroplast MDH, and MDH from Thermus flavus; the other group includes MDHs that are similar to lactate dehydrogenase (LDH). Structure comparisons, the MDHs are mostly dimeric or tetrameric, overview
evolution
-
MDH is a ubiquitous enzyme found in prokaryotic and eukaryotic organisms. The enzyme belongs to the superfamily of 2-ketoacid NAD(P)+-dependent dehydrogenases. MDH has diverged into two distinct phylogenetic groups. One group includes cytoplasmic MDH, chloroplast MDH, and MDH from Thermus flavus; the other group includes MDHs that are similar to lactate dehydrogenase (LDH). Structure comparisons, the MDHs are mostly dimeric or tetrameric, overview
evolution
-
MDH is a ubiquitous enzyme found in prokaryotic and eukaryotic organisms. The enzyme belongs to the superfamily of 2-ketoacid NAD(P)+-dependent dehydrogenases. MDH has diverged into two distinct phylogenetic groups. One group includes cytoplasmic MDH, chloroplast MDH, and MDH from Thermus flavus; the other group includes MDHs that are similar to lactate dehydrogenase (LDH). Structure comparisons, the MDHs are mostly dimeric or tetrameric, overview
evolution
-
MDH is a ubiquitous enzyme found in prokaryotic and eukaryotic organisms. The enzyme belongs to the superfamily of 2-ketoacid NAD(P)+-dependent dehydrogenases. MDH has diverged into two distinct phylogenetic groups. One group includes cytoplasmic MDH, chloroplast MDH, and MDH from Thermus flavus; the other group includes MDHs that are similar to lactate dehydrogenase (LDH). Structure comparisons, the MDHs are mostly dimeric or tetrameric, overview
evolution
-
MDH is a ubiquitous enzyme found in prokaryotic and eukaryotic organisms. The enzyme belongs to the superfamily of 2-ketoacid NAD(P)+-dependent dehydrogenases. MDH has diverged into two distinct phylogenetic groups. One group includes cytoplasmic MDH, chloroplast MDH, and MDH from Thermus flavus, the other group includes MDHs that are similar to lactate dehydrogenase (LDH). Structure comparisons, the MDHs are mostly dimeric or tetrameric, overview
-
evolution
-
MDH is a ubiquitous enzyme found in prokaryotic and eukaryotic organisms. The enzyme belongs to the superfamily of 2-ketoacid NAD(P)+-dependent dehydrogenases. MDH has diverged into two distinct phylogenetic groups. One group includes cytoplasmic MDH, chloroplast MDH, and MDH from Thermus flavus; the other group includes MDHs that are similar to lactate dehydrogenase (LDH). Structure comparisons, the MDHs are mostly dimeric or tetrameric, overview
-
malfunction
Arabidopsis thaliana mutants lacking the NADP-malate dehydrogenase lose the reversible inactivation of catalase activity and the increase in H2O2 levels when exposed to high light. The mutants are slightly affected in growth and accumulate higher levels of NADPH in the chloroplast than the wild-type. Catalase activity and H2O2 levels under high light stress in Arabidopsis thaliana knockout mutants deficient for chloroplastic NADP-MDH, overview
malfunction
-
Arabidopsis thaliana mutants lacking the NADP-malate dehydrogenase lose the reversible inactivation of catalase activity and the increase in H2O2 levels when exposed to high light. The mutants are slightly affected in growth and accumulate higher levels of NADPH in the chloroplast than the wild-type. Catalase activity and H2O2 levels under high light stress in Arabidopsis thaliana knockout mutants deficient for chloroplastic NADP-MDH, overview
-
metabolism
the enzyme is involved in the signalling by a H2O2 pulse in high light-stressed plants, overview The malate valve plays a crucial role in transmitting the redox state of the chloroplast to other cell compartments
metabolism
-
the enzyme is involved in the signalling by a H2O2 pulse in high light-stressed plants, overview The malate valve plays a crucial role in transmitting the redox state of the chloroplast to other cell compartments
-
physiological function
in illuminated chloroplasts, one mechanism involved in reduction oxidation (redox) homeostasis is the malate-oxaloacetate shuttle. Excess electrons from photosynthetic electron transport in the form of nicotinamide adenine dinucleotide phosphate, reduced are used by NADP+-dependent malate dehydrogenase to reduce oxaloacetate to malate, thus regenerating the electron acceptor NADP+. Since NADP-MDH is a strictly redox-regulated, light-activated enzyme that is inactive in the dark, the malate-oxaloacetate shuttle is in the dark or in nonphotosynthetic tissues proposed to be mediated by the constitutively active plastidial NAD-specific MDH isoform (pdNAD-MDH, EC 1.1.1.37), which is is active under both light and dark conditions. pdNAD-MDH deficiency in miR-mdh-1 can be functionally complemented by expression of a microRNA-insensitive pdNAD-MDH but not NADP-MDH, confirming distinct roles for NAD- and NADP-linked redox homeostasis. NADP-MDH is not crucial for providing electron acceptors in chloroplasts
physiological function
-
regulation of MDH activity, overview
physiological function
-
regulation of MDH activity, overview
physiological function
-
regulation of MDH activity, overview
physiological function
-
regulation of MDH activity, overview
physiological function
-
regulation of MDH activity, overview
physiological function
the malate valve plays an essential role in the regulation of catalase activity and the accumulation of a H2O2 signal by transmitting the redox state of the chloroplast to other cell compartments
physiological function
maize enzyme-overexpressing Arabidopsis thaliana plants are tolerant to salt stress (150 mM NaCl)
physiological function
thiol-switch redox regulation of enzyme activity is crucial for maintaining NADPH homeostasis in chloroplasts and plays a crucial role in the optimal growth of plants under short-day or fluctuating light conditions
physiological function
-
the malate valve plays an essential role in the regulation of catalase activity and the accumulation of a H2O2 signal by transmitting the redox state of the chloroplast to other cell compartments
-
physiological function
-
regulation of MDH activity, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
C23A
-
minute activity under oxidizing conditions, up to 1300fold activation under reducing conditions
C23A/C28A
-
minute activity under oxidizing conditions, up to 1300fold activation under reducing conditions
C23A/C28A/C206A
-
only marginal activity in the oxidized state, does not exhibit full activity in the crude extract
C28A
-
minute activity under oxidizing conditions, up to 1300fold activation under reducing conditions
DELTAN
-
mutant lacking the N-terminal 45 residues
C207A
Sorghum sp.
-
strictly thioredoxin-dependent, totally insensitive to diethyl dicarbonate
C207A/DETAEV
Sorghum sp.
-
very low spontaneous activity, high Km-value for oxaloacetate, fast activation kinetics in the presence of reduced thioredoxin, ability to be activated by dithiothreitol alone at a slow rate
C207A/E387Q
Sorghum sp.
-
very low spontaneous activity, high Km-value for oxaloacetate, fast activation kinetics in the presence of reduced thioredoxin, ability to be activated by dithiothreitol alone at a slow rate
C24S/C207A
Sorghum sp.
-
oxidation-reduction midpoint potential is -310 mV at pH 7.0, compared to -330 mV for the wild-type enzyme
C24S/C29S
Sorghum sp.
-
oxidation-reduction midpoint potential is -280 mV at pH 7.0, compared to -330 mV for the wild-type enzyme
C29S
Sorghum sp.
-
strictly thioredoxin-dependent, totally insensitive to diethyl dicarbonate
C29S/C207A
Sorghum sp.
-
no spontaneous activity, activated much faster than the wild-type protein, strictly dependent on reduced thioredoxin for activation
C29S/C207A/DELTAEV
Sorghum sp.
-
high spontaneous activity, activated by reduced thioredoxin almost instantaneously and also by dithiothreitol alone, although at a much slower rate. The Km-values for both the oxidized and reduced enzyme show no significant differences in the apparent affinity for NADPH, whereas the Km for oxaloacetate is dramatically increased in the oxidized form
C29S/C207A/E387Q
Sorghum sp.
-
high spontaneous activity, activated by reduced thioredoxin almost instantaneously and also by dithiothreitol alone, although at a much slower rate. The Km-values for both the oxidized and reduced enzyme show no significant differences in the apparent affinity for NADPH, whereas the Km for oxaloacetate is dramatically increased in the oxidized form
C29S/DELTAEV
Sorghum sp.
-
very low spontaneous activity, high Km-value for oxaloacetate, fast activation kinetics in the presence of reduced thioredoxin, ability to be activated by dithiothreitol alone at a slow rate
C39S/E387Q
Sorghum sp.
-
very low spontaneous activity, high Km-value for oxaloacetate, fast activation kinetics in the presence of reduced thioredoxin, ability to be activated by dithiothreitol alone at a slow rate
C64S
Sorghum sp.
-
still requires activation by reduced thioredoxin, activation is almost instantaneous, whereas the native enzyme reaches full activity after 10-20 min of preincubation, the half-saturation concentration for reduced thioredoxin is decreased 2fold
C64S/C69S
Sorghum sp.
-
still requires activation by reduced thioredoxin, activation is almost instantaneous, whereas the native enzyme reaches full activity after 10-20 min of preincubation, the half-saturation concentration for reduced thioredoxin is decreased 2fold
C69S
Sorghum sp.
-
still requires activation by reduced thioredoxin, activation is almost instantaneous, whereas the native enzyme reaches full activity after 10-20 min of preincubation, the half-saturation concentration for reduced thioredoxin is decreased 2fold
D201A
Sorghum sp.
-
only slightly active, 80fold increased Km for oxaloacetate, Km-value for NADPH is slightly decreased
D201N
Sorghum sp.
-
only slightly active, 45fold increased Km for oxaloacetate, Km-value for NADPH is slightly decreased
DELTAEV
Sorghum sp.
-
mutant with the two most C-terminal residues deleted, NADP+ does not inhibit activation, activation time course of thioredoxin-dependent activation of both mutant proteins is similar to that of the wild-type protein
DELTAN
Sorghum sp.
-
truncation mutant corresponding to the deletion of the 5' end of the mdh cDNA open reading frame until the 73rd codon
E387Q
Sorghum sp.
-
NADP+ does not inhibit activation, activation time course of thioredoxin-dependent activation of both mutant proteins is similar to that of the wild-type protein
G84D
Sorghum sp.
-
10fold lower Km for NADH, Km for NADPH remains unchanged
G84D/S851I/R87Q/S88A
Sorghum sp.
-
changed cofactor specificity from NADPH to NADH, the activation of the NAD-specific thiol-regulated enzyme is inhibited by NAD+ but no longer by NADP+
H229N
Sorghum sp.
-
no activity
H229Q
Sorghum sp.
-
no activity
S85I/R87Q/S88A
Sorghum sp.
-
7fold increase in the Km-value for NADPH and 4fold decrease in Km-value for NADH
additional information
-
no promoter elements are identified in 5' direction of the NADP-MDH gene. It is concluded that in Brassicaceae the majority of regulatory elements are located within the coding region
additional information
-
no promoter elements are identified in 5' direction of the NADP-MDH gene, and the expression of NADP-MDH is not affected in knock-out plants carrying a DNA insert in the 5'region. It is concluded that in Brassicaceae the majority of regulatory elements are located within the coding region
additional information
two Arabidopsis thaliana nadp-mdh T-DNA insertion mutants M44 and M81 are compared with the isogenic wild-type S44 segregated from the parent heterozygous plant of M44 initially identified by PCR genotyping
additional information
-
two Arabidopsis thaliana nadp-mdh T-DNA insertion mutants M44 and M81 are compared with the isogenic wild-type S44 segregated from the parent heterozygous plant of M44 initially identified by PCR genotyping
-
additional information
-
no promoter elements are identified in 5' direction of the NADP-MDH gene. It is concluded that in Brassicaceae the majority of regulatory elements are located within the coding region
additional information
-
no promoter elements are identified in 5' direction of the NADP-MDH gene. It is concluded that in Brassicaceae the majority of regulatory elements are located within the coding region
additional information
-
no promoter elements are identified in 5' direction of the NADP-MDH gene. It is concluded that in Brassicaceae the majority of regulatory elements are located within the coding region
additional information
-
no promoter elements are identified in 5' direction of the NADP-MDH gene. It is concluded that in Brassicaceae the majority of regulatory elements are located within the coding region
additional information
-
no promoter elements are identified in 5' direction of the NADP-MDH gene. It is concluded that in Brassicaceae the majority of regulatory elements are located within the coding region
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Isegawa, Y.; Nakano, Y.; Kitaoka, S.
Submitochondrial location and some properties of NAD+- and NADP+-linked malate dehydrogenase in Euglena
Agric. Biol. Chem.
48
549-552
1984
Euglena gracilis, Euglena gracilis SM-ZK
-
brenda
Johnson, H.S.
NADP-malate dehydrogenase: photoactivation in leaves of plants with Calvin cycle photosynthesis
Biochem. Biophys. Res. Commun.
43
703-709
1971
Hordeum vulgare, Spinacia oleracea
brenda
Luchetta, P.; Cretin, C.; Gadal, P.
Structure and characterization of the Sorghum vulgare gene encoding NADP-malate dehydrogenase
Gene
89
171-177
1990
Sorghum bicolor
brenda
Agostino, A.; Jeffrey, P.; Hatch, M.D.
Amino acid sequence and molecular weight of native NADP malate dehydrogenase from the C4 plant Zea mays
Plant Physiol.
98
1506-1510
1992
Zea mays
brenda
Vairinhos, F.; Simon, J.P.
Purification and molecular forms of NADP+-malate dehydrogenase from two populations of the C4 weed Echinochloa crus-galli (L.) Beauv. (Poaceae)
Plant Sci.
71
173-177
1990
Echinochloa crus-galli
-
brenda
Miginiac-Maslow, M.; Decottignies, P.; Jacquot, J.P.; Gadal, P.
Regulation of corn leaf NADP-malate dehydrogenase light-activation by the photosynthetic electron flow. Effect of photoinhibition studied in a reconstituted system
Biochim. Biophys. Acta
1017
273-279
1990
Pisum sativum, Spinacia oleracea, Zea mays
-
brenda
Scheibe, R.; Rudolph, R.; Reng, W.; Jaenicke, R.
Structural and catalytic properties of oxidized and reduced chloroplast NADP-malate dehydrogenase upon denaturation and renaturation
Eur. J. Biochem.
189
581-587
1990
Pisum sativum
brenda
Cheng, S.H.; Moore, B.D.; Edwards, G.E.; Ku, M.S.B.
Photosynthesis in Flaveria brownii, a C4-like species. Leaf anatomy, characterization of CO2, exchange, compartmentation of photosynthetic enzymes, and metabolism of 14CO2
Plant Physiol.
87
867-873
1988
Flaveria brownii
brenda
Migniac-Maslow, M.; Cornic, G.; Jacquot, J.P.
Effect of high light intensities on oxygen evolution and the light activation of NADP-malate dehydrogenase in intact spinach chloroplasts
Planta
173
468-473
1988
Spinacia oleracea
brenda
Fickenscher, K.; Scheibe, R.
Limited proteolysis of inactive tetrameric chloroplast NADP-malate dehydrogenase produces active dimers
Arch. Biochem. Biophys.
260
771-779
1988
Pisum sativum
brenda
Kagawa, T.; Bruno, P.L.
NADP-malate dehydrogenase from leaves of Zea mays: purification and physical, chemical, and kinetic properties
Arch. Biochem. Biophys.
260
674-695
1988
Zea mays
brenda
Jawali, N.; Bhagwat, A.S.
Presence of essential histidine residues in NADP-malic enzyme from maize
Phytochemistry
26
1859-1862
1987
Zea mays
-
brenda
Krimm, I.; Goyer, A.; Issakidis-Bourguet, E.; Miginiac-Maslow, M.; Lancelin, J.M.
Direct NMR observation of the thioredoxin-mediated reduction of the chloroplast NADP-malate dehydrogenase provides a structural basis for the relief of autoinhibition
J. Biol. Chem.
274
34539-34542
1999
Sorghum bicolor
brenda
Scheibe, R.; Wagenpfeil, D.; Fischer, J.
NADP-malate dehydrogenase activity during photosynthesis in illuminated spinach chloroplasts
J. Plant Physiol.
124
103-110
1986
Spinacia oleracea
-
brenda
Jacquot, J.P.; Decottignies, P.
Further evidence for a role of sulfhydryl in the thioredoxin dependent activation of corn NADP-malate dehydrogenase
FEBS Lett.
209
87-91
1986
Zea mays
-
brenda
Nakamoto, H.; Edwards, G.E.
Light activation of pyruvate, Pi dikinase and NADP-malate dehydrogenase in mesophyll protoplasts in maize
Plant Physiol.
82
312-315
1986
Zea mays
brenda
Edwards, G.E.; Nakamoto, H.; Burnell, J.N.; Hatch, M.D.
Pyruvate, Pi dikinase and NADP-malate dehydrogenase in C4 photosynthesis: properties and mechanism of light/dark regulation
Annu. Rev. Plant Physiol.
36
255-286
1985
Pisum sativum, Zea mays
-
brenda
Scheibe, R.; Fickenscher, K.; Ashton, A.R.
Studies on the mechanism of the reductive activation of NADP-malate dehydrogenase by thioredoxin m and low-molecular-weight thiols
Biochim. Biophys. Acta
870
191-197
1986
Pisum sativum
-
brenda
Ferte, N.; Jaquot, J.P.; Meunier, J.C.
Structural, immunological and kinetic comparisons of NADP-dependent malate dehydrogenases from spinach (C3) and corn (C4) chloroplasts
Eur. J. Biochem.
154
587-595
1986
Spinacia oleracea, Zea mays
brenda
Gotow, K.; Tanaka, K.; Kondo, N.; Kobayashi, K.; Syono, K.
Light activation of NADP-malate dehydrogenase in guard cell protoplasts from Vicia faba L.
Plant Physiol.
79
829-832
1985
Vicia faba
brenda
Ferte, N.; Meunier, J.C.
Purification of several NADP-dependent malate dehydrogenase isoenzymes from spinach leaves. Kinetic properties
Plant Sci. Lett.
37
115-121
1984
Spinacia oleracea
-
brenda
Wolosiuk, R.A.; Buchanan, B.B.; Crawford, N.A.
Regulation of NADP-malate dehydrogenase by light-actuated ferredoxin/thioredoxin system of chloroplasts
FEBS Lett.
81
253-258
1977
Spinacia oleracea
-
brenda
Scheibe, R.; Fickenscher, K.
The dark (oxidized) form of the light-activatable NADP-malate dehydrogenase from pea chloroplasts is catalytically active in the presence of guanidine-HCl
FEBS Lett.
180
317-320
1985
Pisum sativum
-
brenda
Perrot-Rechenmann, C.; Jacquot, J.P.; Gadal, P.; Weeden, N.F.; Cseke, C.; Buchanan, B.B.
Localization of NADP-malate dehydrogenase of corn leaves by immunological methods
Plant Sci. Lett.
30
219-226
1983
Zea mays
-
brenda
Scheibe, R.; Jacquot, J.P.
NADP regulates the light activation of NADP-dependent malate dehydrogenase
Planta
157
548-553
1983
Pisum sativum
brenda
Fickenscher, K.; Scheibe, R.
Purification and properties of NADP-dependent malate dehydrogenase from pea leaves
Biochim. Biophys. Acta
749
249-254
1983
Pisum sativum
-
brenda
Ferte, N.; Meunier, J.C.; Ricard, J.; Buc, J.; Sauve, P.
Molecular properties and thioredoxin-mediated activation of spinach chloroplastic NADP-malate dehydrogenase
FEBS Lett.
146
133-138
1982
Spinacia oleracea
-
brenda
Jacquot, J.P.P.; Buchanan, B.B.; Martin, F.; Vidal, J.
Enzyme regulation in C4 photosynthesis. Purification and properties of thioredoxin-linked NADP-malate dehydrogenase from corn leaves
Plant Physiol.
68
300-304
1981
Zea mays
brenda
Mohamed, A.H.; Anderson, L.E.
Extraction of chloroplast light effect mediator(s) and reconstitution of light activation of NADP-linked malate dehydrogenase
Arch. Biochem. Biophys.
209
606-612
1981
Pisum sativum
brenda
Cretin, C.; Luchetta, P.; Joly, C.; Decottignies, P.; Lepiniec, L.; Gadal, P.; Sallantin, M.; Huet, J.C.; Pernollet, J.C.
Primary structure of sorghum malate dehydrogenase (NADP) deduced from cDNA sequence. Homology with malate dehydrogenase (NAD)
Eur. J. Biochem.
192
299-303
1990
Sorghum bicolor
brenda
Johansson, K.; Ramaswamy, S.; Saarinen, M.; Lemaire-Chamley, M.; Issakidis-Bourguet, E.; Miginiac-Maslow, M.; Eklund, H.
Structural basis for light activation of a chloroplast enzyme: The structure of Sorghum NADP-malate dehydrogenase in its oxidized form
Biochemistry
38
4319-4326
1999
Sorghum bicolor (P17606)
brenda
MacPherson, K.H.; Ashton, A.R.; Carr, P.D.; Trevanion, S.J.; Verger, D.; Ollis, D.L.
Crystallization and preliminary crystallographic studies of chloroplast NADP-dependent malate dehydrogenase from Flaveria bidentis
Acta Crystallogr. Sect. D
54
654-656
1998
Flaveria bidentis
brenda
Hatch, M.D.; Slack, C.R.
NADPH-specific malate dehydrogenase and glycerate kinase in leaves and evidence for their location in chloroplasts
Biochem. Biophys. Res. Commun.
34
589-593
1969
Amaranthus palmeri, Beta vulgaris, Daucus carota, Pisum sativum, Saccharum sp., Spinacia oleracea, Zea mays
brenda
Scheibe, R.; Geissler, A.; Rother, T.
Analysis of biophysical differences between oxidized and reduced chloroplast NADP-malate dehydrogenase
Arch. Biochem. Biophys.
300
635-640
1993
Pisum sativum, Spinacia oleracea
brenda
Kampfenkel, K.
Limited proteolysis of NADP-malate dehydrogenase from pea chloroplast by aminopeptidase K yields monomers. Evidence of proteolytic degradation of NADP-malate dehydrogenase during purification from pea
Biochim. Biophys. Acta
1156
71-77
1992
Pisum sativum
brenda
Riessland, R.; Jaenicke, R.
Determination of the regulatory disulfide bonds of NADP-dependent malate dehydrogenase from Pisum sativum by site-directed mutagenesis
Biol. Chem.
378
983-988
1997
Pisum sativum
brenda
Gupta, V.K.; Singh, R.
Properties of NADP+-malate dehydrogenase from immature pod wall of Cicer arietinum
Plant Physiol. Biochem.
28
671-678
1990
Cicer arietinum
-
brenda
Issakidis, E.; Miginiac-Maslow, M.; Decottignies, P.; Jacquot, J.P.; Cretin, C.; Gadal, P.
Site-directed mutagenesis reveals the involvement of an additional thioredoxin-dependent regulatory site in the activation of recombinant sorghum leaf NADP-malate dehydrogenase
J. Biol. Chem.
267
21577-21583
1992
Sorghum sp.
brenda
Ruelland, E.; Johansson, K.; Decottignies, P.; Djukic, N.; Miginiac-Maslow, M.
The autoinhibition of sorghum NADP malate dehydrogenase is mediated by a C-terminal negative charge
J. Biol. Chem.
273
33482-33488
1998
Sorghum sp.
brenda
Carr, P.D.; Verger, D.; Ashton, A.R.; Ollis, D.L.
Chloroplast NADP-malate dehydrogenase: structural basis of light-dependent regulation of activity by thiol oxidation and reduction
Structure
7
461-475
1999
Flaveria bidentis
brenda
Schepens, I.; Decottignies, P.; Ruelland, E.; Johansson, K.; Miginiac-Maslow, M.
The dimer contact area of sorghum NADP-malate dehydrogenase: role of aspartate 101 in dimer stability and catalytic activity
FEBS Lett.
471
240-244
2000
Sorghum sp.
brenda
Hirasawa, M.; Ruelland, E.; Schepens, I.; Issakidis-Bourguet, E.; Miginiac-Maslow, M.; Knaff, D.B.
Oxidation-reduction properties of the regulatory disulfides of sorghum chloroplast nicotinamide adenine dinucleotide phosphate-malate dehydrogenase
Biochemistry
39
3344-3350
2000
Sorghum bicolor, Sorghum sp.
brenda
Jacquot, J.P.; Keryer, E.; Issakidis, E.; Decottignies, P.; Miginiac-Maslow, M.; Schmitter, J.M.; Cretin, C.
Properties of recombinant NADP-malate dehydrogenases from Sorghum vulgare leaves expressed in Escherichia coli cells
Eur. J. Biochem.
199
47-51
1991
Sorghum bicolor
brenda
Braun, H.; Lichter, A.; Haberlein, I.
Kinetic evidence for protein complexes between thioredoxin and NADP-malate dehydrogenase and presence of a thioredoxin binding site at the N-terminus of the enzyme
Eur. J. Biochem.
240
781-788
1996
Glycine max
brenda
Lemaire, M.; Miginiac-Maslow, M.; Decottignies, P.
The catalytic site of chloroplastic NADP-dependent malate dehydrogenase contains a His/Asp pair
Eur. J. Biochem.
236
947-952
1996
Sorghum sp.
brenda
Gomez, I.; Merchan, F.; Fernandez, E.; Quesada, A.
NADP-malate dehydrogenase from Chlamydomonas: prediction of new structural determinants for redox regulation by homology modelling
Plant Mol. Biol.
48
211-221
2002
Chlamydomonas reinhardtii (Q9FNS5)
brenda
Rondeau, P.; Rouch, C.; Besnard, G.
NADP-malate dehydrogenase gene evolution in Andropogoneae (Poaceae): gene duplication followed by sub-functionalization
Ann. Bot.
96
1307-1314
2005
Oryza sativa, Zea mays (P15719), Sorghum bicolor (P17606), Sorghum bicolor (P37229), Saccharum officinarum (Q1RS10), Saccharum officinarum (Q8L6C8), Setaria geminata (Q1RS11), Heteropogon contortus (Q2MG92), Melinis repens (Q2MG93), Hyparrhenia rufa (Q2MG94), Flaveria trinervia (Q42737), Saccharum hybrid cultivar R570 (Q4W4C2), Chrysopogon zizanioides (Q8H0J7), Chrysopogon zizanioides (Q8L5S9), Themeda quadrivalvis (Q8H0K0), Sorghum arundinaceum (Q8H0L7), Saccharum spontaneum (Q8H0M0), Pogonatherum paniceum (Q8H0N4), Paspalum paniculatum (Q8H0N5), Megathyrsus maximus (Q8H0N9), Oplismenus compositus (Q8H0P4), Ischaemum koleostachys (Q8H0Q3), Dichanthium aristatum (Q8H0R5)
brenda
Lemaire, S.D.; Quesada, A.; Merchan, F.; Corral, J.M.; Igeno, M.I.; Keryer, E.; Issakidis-Bourguet, E.; Hirasawa, M.; Knaff, D.B.; Miginiac-Maslow, M.
NADP-malate dehydrogenase from unicellular green alga Chlamydomonas reinhardtii. A first step toward redox regulation?
Plant Physiol.
137
514-521
2005
Chlamydomonas reinhardtii (Q9FNS5)
brenda
Zhang, C.; Chen, L.; Shi, D.; Chen, G.; Lu, C.; Wang, P.; Wang, J.; Chu, H.; Zhou, Q.; Zuo, M.; Sun, L.
Characteristics of ribulose-1,5-bisphosphate carboxylase and C4 pathway key enzymes in flag leaves of a super-high-yield hybrid rice and its parents during the reproductive stage
S. Afr. J. Bot.
73
22-28
2007
Oryza sativa
-
brenda
Hameister, S.; Becker, B.; Holtgrefe, S.; Strodtkoetter, I.; Linke, V.; Backhausen, J.E.; Scheibe, R.
Transcriptional regulation of NADP-dependent malate dehydrogenase: comparative genetics and identification of DNA-binding proteins
J. Mol. Evol.
65
437-455
2007
Arabidopsis thaliana, Capsella bursa-pastoris, Cochlearia officinalis, Capsella rubella, Arabidopsis lyrata subsp. petraea, Lepidium densiflorum, Lepidium latifolium
brenda
Anderson, L.E.; Fadowole, D.; Reyes, B.A.; Carol, A.A.
Distribution of thioredoxins f and m with respect to seven light-activated enzymes and three redox-insensitive proteins in pea leaf chloroplasts
Plant Sci.
174
432-445
2008
Pisum sativum
brenda
Kawakami, R.; Sakuraba, H.; Goda, S.; Tsuge, H.; Ohshima, T.
Refolding, characterization and crystal structure of (S)-malate dehydrogenase from the hyperthermophilic archaeon Aeropyrum pernix
Biochim. Biophys. Acta
1794
1496-1504
2009
Aeropyrum pernix (Q9YEA1)
brenda
Libik-Konieczny, M.; Surowka, E.; Nosek, M.; Goraj, S.; Miszalski, Z.
Pathogen-induced changes in malate content and NADP-dependent malic enzyme activity in C3 or CAM performing Mesembryanthemum crystallinum L. plants
Acta Physiol. Plant.
34
1471-1477
2012
Mesembryanthemum crystallinum
-
brenda
Dulermo, T.; Lazar, Z.; Dulermo, R.; Rakicka, M.; Haddouche, R.; Nicaud, J.M.
Analysis of ATP-citrate lyase and malic enzyme mutants of Yarrowia lipolytica points out the importance of mannitol metabolism in fatty acid synthesis
Biochim. Biophys. Acta
1851
1107-1117
2015
no activity in Yarrowia lipolytica
brenda
Heyno, E.; Innocenti, G.; Lemaire, S.D.; Issakidis-Bourguet, E.; Krieger-Liszkay, A.
Putative role of the malate valve enzyme NADP-malate dehydrogenase in H2O2 signalling in Arabidopsis
Philos. Trans. R. Soc. Lond. B Biol. Sci.
369
20130228
2014
Arabidopsis thaliana (Q8H1E2), Arabidopsis thaliana Col-0 (Q8H1E2)
brenda
Takahashi-Iniguez, T.; Aburto-Rodriguez, N.; Vilchis-Gonzalez, A.; Flores, M.
Function, kinetic properties, crystallization, and regulation of microbial malate dehydrogenase
J. Zhejiang Univ. Sci. B
17
247-261
2016
Aeropyrum pernix, Bacillus subtilis, Thermus thermophilus, Methanothermobacter thermautotrophicus, Methanocaldococcus jannaschii, Pseudomonas putida, Thermus thermophilus AT-62, Bacillus subtilis B1
-
brenda
Beeler, S.; Liu, H.C.; Stadler, M.; Schreier, T.; Eicke, S.; Lue, W.L.; Truernit, E.; Zeeman, S.C.; Chen, J.; Koetting, O.
Plastidial NAD-dependent malate dehydrogenase is critical for embryo development and heterotrophic metabolism in Arabidopsis
Plant Physiol.
164
1175-1190
2014
Arabidopsis thaliana (Q8H1E2)
brenda
Yokochi, Y.; Yoshida, K.; Hahn, F.; Miyagi, A.; Wakabayashi, K.I.; Kawai-Yamada, M.; Weber, A.P.M.; Hisabori, T.
Redox regulation of NADP-malate dehydrogenase is vital for land plants under fluctuating light environment
Proc. Natl. Acad. Sci. USA
118
e2016903118
2021
Arabidopsis thaliana (Q8H1E2)
brenda
Kandoi, D.; Mohanty, S.; Tripathy, B.C.
Overexpression of plastidic maize NADP-malate dehydrogenase (ZmNADP-MDH) in Arabidopsis thaliana confers tolerance to salt stress
Protoplasma
255
547-563
2018
Zea mays (P15719)
brenda