Activating Compound | Comment | Organism | Structure |
---|---|---|---|
fumarate | mitochondrial NAD(P)+-dependent malic enzyme (m-NAD(P)-ME) is allosterically activated by fumarate | Homo sapiens | |
additional information | cytosolic NADP+-dependent malic enzyme (c-NADP-ME) is neither a cooperative nor an allosteric enzyme | Homo sapiens |
Cloned (Comment) | Organism |
---|---|
recombinant expression of C-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3) | Homo sapiens |
Protein Variants | Comment | Organism |
---|---|---|
K57S/E59N/K73E/D102S | site-directed mutagenesis | Homo sapiens |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | cytosolic NADP+-dependent malic enzyme (c-NADP-ME) is neither a cooperative nor an allosteric enzyme | Homo sapiens | |
0.3 | - |
NADH | pH 7.4, 30°C, recombinant mutant K57S/E59N/K73E/D102S | Homo sapiens | |
0.3 | - |
NADH | pH 7.4, 30°C, recombinant mutant K57S/E59N/K73E/D102S with 5 mM fumarate | Homo sapiens | |
0.3 | - |
NADH | pH 7.4, 30°C, recombinant wild-type with 5 mM fumarate | Homo sapiens | |
1.4 | - |
NADH | pH 7.4, 30°C, recombinant wild-type | Homo sapiens | |
3 | - |
(S)-malate | pH 7.4, 30°C, recombinant mutant K57S/E59N/K73E/D102S | Homo sapiens | |
3.6 | - |
(S)-malate | pH 7.4, 30°C, recombinant mutant K57S/E59N/K73E/D102S with 5 mM fumarate | Homo sapiens | |
4.6 | - |
(S)-malate | pH 7.4, 30°C, recombinant wild-type enzyme with 5 mM fumarate | Homo sapiens | |
15.6 | - |
(S)-malate | pH 7.4, 30°C, recombinant wild-type enzyme | Homo sapiens |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
cytosol | - |
Homo sapiens | 5829 | - |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
(S)-malate + NAD+ | Homo sapiens | - |
pyruvate + CO2 + NADH | - |
r |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | P23368 | - |
- |
Purification (Comment) | Organism |
---|---|
recombinant C-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, dialysis, and ultrafiltration | Homo sapiens |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
(S)-malate + NAD+ | - |
Homo sapiens | pyruvate + CO2 + NADH | - |
r |
Subunits | Comment | Organism |
---|---|---|
dimer and tetramer | - |
Homo sapiens |
Synonyms | Comment | Organism |
---|---|---|
m-NAD(P)-ME | - |
Homo sapiens |
mitochondrial NAD(P)+-dependent malic enzyme | - |
Homo sapiens |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | - |
assay at | Homo sapiens |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
5 | - |
(S)-malate | pH 7.4, 30°C, recombinant mutant K57S/E59N/K73E/D102S with or without 5 mM fumarate | Homo sapiens | |
43 | - |
(S)-malate | pH 7.4, 30°C, recombinant wild-type enzyme | Homo sapiens | |
55 | - |
(S)-malate | pH 7.4, 30°C, recombinant wild-type enzyme with 5 mM fumarate | Homo sapiens |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.4 | - |
assay at | Homo sapiens |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
additional information | the isoenzyme can also use NADP+ but is more effective with NAD+ | Homo sapiens | |
NAD+ | - |
Homo sapiens | |
NADH | - |
Homo sapiens | |
NADP+ | - |
Homo sapiens | |
NADPH | - |
Homo sapiens |
General Information | Comment | Organism |
---|---|---|
additional information | the molecular basis for the different allosteric properties and quaternary structural stability of m-NAD(P)-ME, EC 1.1.1.38 and c-NADP-ME, EC 1.1.1.40. The structural features near the fumarate binding site and the dimer interface are highly related to the quaternary structural stability of c-NADP-ME and m-NAD(P)-ME. Lys57 plays functional roles in both the allosteric regulation and the subunit-subunit interaction of humanm-NAD(P)-ME | Homo sapiens |