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Literature summary for 1.1.1.38 extracted from

  • Hsieh, J.; Li, S.; Chen, M.; Yang, P.; Chen, H.; Chan, N.; Liu, J.; Hung, H.
    Structural characteristics of the nonallosteric human cytosolic malic enzyme (2014), Biochim. Biophys. Acta, 1844, 1773-1783.
    View publication on PubMed

Activating Compound

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(Commentary)

Cloned (Comment) Organism
recombinant expression of C-terminally His6-tagged enzyme in Escherichia coli strain BL21(DE3) Homo sapiens

Protein Variants

Protein Variants Comment Organism
K57S/E59N/K73E/D102S site-directed mutagenesis Homo sapiens

KM Value [mM]

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

Localization Comment Organism GeneOntology No. Textmining
cytosol
-
Homo sapiens 5829
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
(S)-malate + NAD+ Homo sapiens
-
pyruvate + CO2 + NADH
-
r

Organism

Organism UniProt Comment Textmining
Homo sapiens P23368
-
-

Purification (Commentary)

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 and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(S)-malate + NAD+
-
Homo sapiens pyruvate + CO2 + NADH
-
r

Subunits

Subunits Comment Organism
dimer and tetramer
-
Homo sapiens

Synonyms

Synonyms Comment Organism
m-NAD(P)-ME
-
Homo sapiens
mitochondrial NAD(P)+-dependent malic enzyme
-
Homo sapiens

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
assay at Homo sapiens

Turnover Number [1/s]

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

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.4
-
assay at Homo sapiens

Cofactor

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

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