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Literature summary for 1.1.1.82 extracted from

  • 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 (1998), J. Biol. Chem., 273, 33482-33488.
    View publication on PubMed
Search for more literature for 1.1.1.82

Activating Compound

Activating Compound Comment Organism Structure
thioredoxin activated by thiol/disulfide interchange with reduced thioredoxin Sorghum sp.

Protein Variants

Protein Variants Comment Organism
C207A strictly thioredoxin-dependent, totally insensitive to diethyl dicarbonate Sorghum sp.
C207A/DETAEV 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 Sorghum sp.
C207A/E387Q 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 Sorghum sp.
C29S strictly thioredoxin-dependent, totally insensitive to diethyl dicarbonate Sorghum sp.
C29S/C207A no spontaneous activity, activated much faster than the wild-type protein, strictly dependent on reduced thioredoxin for activation Sorghum sp.
C29S/C207A/DELTAEV 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 Sorghum sp.
C29S/C207A/E387Q 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 Sorghum sp.
C29S/DELTAEV 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 Sorghum sp.
C39S/E387Q 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 Sorghum sp.
DELTAEV 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 Sorghum sp.
E387Q 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 Sorghum sp.

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.029
-
 NADPH mutant enzyme C207A/E387Q, oxidized form Sorghum sp.
0.031
-
 NADPH mutant enzyme C29S/C207A/E387Q, oxidized enzyme form Sorghum sp.
0.035
-
 NADPH mutant enzyme C29S/C207A/DELTAEV, oxidized form Sorghum sp.
0.044
-
 NADPH mutant enzyme C29S/E387Q, reduced form Sorghum sp.
0.046
-
 NADPH mutant enzyme C29S/E387Q, reduced form Sorghum sp.
0.047
-
 NADPH mutant enzyme C207A/DELTAEV, oxidized form Sorghum sp.
0.049
-
 NADPH mutant enzyme C29S/DELTAEV, oxidized form Sorghum sp.
0.05
-
 oxaloacetate mutant enzyme C39S/E387Q, reduced form Sorghum sp.
0.054
-
 oxaloacetate mutant enzyme C207A/DELTAEV, reduced form Sorghum sp.
0.056
-
 oxaloacetate mutant enzyme C29S/E387Q, reduced form Sorghum sp.
0.06
-
 NADPH mutant enzyme C207A/DELTAEV, and mutant enzyme C29S/C207S/DELTAEV, reduced forms Sorghum sp.
0.063
-
 NADPH mutant enzyme C29S/DELTAEV, reduced form Sorghum sp.
0.066
-
 NADPH mutant enzyme C29S/C207A/E387Q, reduced form and mutant enzyme C29S/C207A/DELTAEV, reduced form Sorghum sp.
0.07
-
 oxaloacetate mutant enzyme C29S/DELTAEV, reduced form Sorghum sp.
0.086
-
 oxaloacetate mutant enzyme C29S/C207A/E387Q, reduced form Sorghum sp.
0.094
-
 oxaloacetate mutant enzyme C29S/C207A, reduced form Sorghum sp.
0.115
-
 NADPH mutant enzyme C29S/C207A, reduced form Sorghum sp.
0.447
-
 oxaloacetate mutant enzyme C207A/DELTAEV, oxidized form Sorghum sp.
0.578
-
 oxaloacetate mutant enzyme C29S/DELTAEV, oxidized form Sorghum sp.
0.583
-
 oxaloacetate mutant enzyme C29S/E387Q, oxidized form Sorghum sp.
0.894
-
 oxaloacetate mutant enzyme C29S/C207A/E387Q, oxidized form Sorghum sp.
0.931
-
 oxaloacetate mutant enzyme C29S/C207A/DELTAEV, oxidized form Sorghum sp.

Localization

Localization Comment Organism GeneOntology No. Textmining
chloroplast
-
 Sorghum sp. 9507
-

Organism

Organism UniProt Comment Textmining
Sorghum sp.
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
oxaloacetate + NADPH
-
 Sorghum sp. (S)-malate + NADP+
-
 ?