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Literature summary extracted from

  • Chang, H.C.; Chen, L.Y.; Lu, Y.H.; Li, M.Y.; Chen, Y.H.; Lin, C.H.; Chang, G.G.
    Metal ions stabilize a dimeric molten globule state between the open and closed forms of malic enzyme (2007), Biophys. J., 93, 3977-3988.
    View publication on PubMedView publication on EuropePMC

Protein Variants

EC Number Protein Variants Comment Organism
1.1.1.40 W252A site-directed mutagenesis, the mutant is no longer protected by Mn2+ against denaturation by urea and digestion by trypsin Columba sp.
1.1.1.40 W252F site-directed mutagenesis, the mutant is no longer protected by Mn2+ against denaturation by urea and digestion by trypsin Columba sp.
1.1.1.40 W252H site-directed mutagenesis, the mutant is no longer protected by Mn2+ against denaturation by urea and digestion by trypsin Columba sp.
1.1.1.40 W252I site-directed mutagenesis, the mutant is no longer protected by Mn2+ against denaturation by urea and digestion by trypsin Columba sp.
1.1.1.40 W252S site-directed mutagenesis, the mutant is no longer protected by Mn2+ against denaturation by urea and digestion by trypsin Columba sp.

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.1.1.39 Urea denaturation, in 3-5 M urea, the enzyme undergoes a reversible tetramer-dimer-monomer quaternary structural change in an acidic pH environment, which resulted in a molten globule state that is prone to aggregate, Mn2+ protects, overview Homo sapiens
1.1.1.40 Trypsin digests the mutant enzymes, while the wild-type enzyme is protected in the presence of Mn2+, because a specific cutting site in the Lys352-Gly-Arg354 region is able to generate a unique polypeptide with Mr of 37 kDa, and this polypeptide is resistant to further digestion Columba sp.
1.1.1.40 Urea inactivation at 3-5 M urea, the pigeon cytosolic NADP+-dependent malic enzyme unfolds and aggregates into various forms with dimers as the basic unit, under the same denaturing conditions but in the presence of 4 mM Mn2+, the enzyme exists exclusively as a molten globule dimer in solution, overview Columba sp.

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.1.1.39 mitochondrion
-
 Homo sapiens 5739
-
1.1.1.40 cytosol
-
 Columba sp. 5829
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.1.1.39 Mn2+ during the catalytic process of malic enzyme, binding of metal ion induces a conformational change within the enzyme from the open form to an intermediate form, which upon binding of L-malate, transforms further into a catalytically competent closed form Homo sapiens
1.1.1.40 Mn2+ required for activity and protective against inactivation and degeneration by urea or digestion by trypsin, Trp252 is involved, overview, during the catalytic process of malic enzyme, binding of metal ion induces a conformational change within the enzyme from the open form to an intermediate form, which upon binding of L-malate, transforms further into a catalytically competent closed form Columba sp.

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.1.39 (S)-malate + NAD+ Homo sapiens
-
 pyruvate + CO2 + NADH
-
 r
1.1.1.40 (S)-malate + NADP+ Columba sp.
-
 pyruvate + CO2 + NADPH
-
 r

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.39 Homo sapiens
-
-
-
1.1.1.40 Columba sp.
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.39 (S)-malate + NAD+
-
 Homo sapiens pyruvate + CO2 + NADH
-
 r
1.1.1.40 (S)-malate + NADP+
-
 Columba sp. pyruvate + CO2 + NADPH
-
 r
1.1.1.40 (S)-malate + NADP+ during the catalytic process of malic enzyme, binding metal ion induces a conformational change within the enzyme from the open form to an intermediate form, which upon binding of L-malate, transforms further into a catalytically competent closed form, overview Columba sp. pyruvate + CO2 + NADPH
-
 r

Subunits

EC Number Subunits Comment Organism
1.1.1.39 tetramer structure analysis from crystal structure, the enzyme is a tetrameric protein with double dimer quaternary structure, pH dependence of enzyme structure, overview Homo sapiens
1.1.1.40 More at 3-5 M urea, the pigeon cytosolic NADP+-dependent malic enzyme unfolds and aggregates into various forms with dimers as the basic unit, under the same denaturing conditions but in the presence of 4 mM Mn2+, the enzyme exists exclusively as a molten globule dimer in solution, aggregation of the enzyme is attributable to the Trp572 side chain, overview Columba sp.
1.1.1.40 tetramer structure analysis from crystal structure, the enzyme is a tetrameric protein with double dimer quaternary structure, pH dependence of enzyme structure, overview Columba sp.

Synonyms

EC Number Synonyms Comment Organism
1.1.1.39 mitochondrial NAD+-dependent malic enzyme
-
 Homo sapiens
1.1.1.40 NADP+-dependent malic enzyme
-
 Columba sp.

pH Range

EC Number pH Minimum pH Maximum Comment Organism
1.1.1.39 additional information
-
 enzyme conformation at different pH values, overview Homo sapiens
1.1.1.40 additional information
-
 enzyme conformation at different pH values, overview Columba sp.

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.39 NAD+
-
 Homo sapiens
1.1.1.39 NADH
-
 Homo sapiens
1.1.1.40 NADP+
-
 Columba sp.
1.1.1.40 NADPH
-
 Columba sp.