Any feedback?
Literature summary for 1.1.1.40 extracted from
- Characterization of malic enzyme and the regulation of its activity and metabolic engineering on lipid production (2015), RSC Adv., 5, 45558-45570.
No PubMed abstract available
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| acetyl phosphate | - |
Escherichia coli |  |
| D-glucose 6-phosphate | - |
Escherichia coli | |
| L-aspartate | - |
Escherichia coli | |
| L-glutamate | - |
Escherichia coli | |
| additional information | the regulation of MaeB activities appears to correlate to the activation of the reverse or forward PTA reaction (interconversion of acetyl-CoA and acetyl-P) | Escherichia coli |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene maeB, sequence comparisons, recombinant expression in Escherichia coli strain BL21 resulting in increased malic enzyme activity and a 4fold enhancement in lipid content. Overexpressing the NADP-ME of Escherichia coli strain BL21 results in a 15% decrease in fatty acid production instead | Escherichia coli |
| sequence comparisons | Rhodotorula toruloides |
| sequence comparisons | Cunninghamella bainieri |
| sequence comparisons, recombinant expression in Mortierella alpine | Mortierella alpina |
| sequence comparisons,, recombinant expressionin Mucor circinelloides | Mucor circinelloides |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| 1-methylenecyclopropan-trans-2,3-dicarboxylic acid | - |
Mucor circinelloides | |
| 1-methylenecyclopropane | inhibits at 10 mM | Mucor circinelloides | |
| acetyl-CoA | - |
Escherichia coli | |
| Glutarate | inhibits at 10 mM | Mucor circinelloides | |
| glyoxylate | competitive inhibition | Mortierella alpina | |
| oxaloacetate | feedback inhibition | Mortierella alpina | |
| sesamol | - |
Mucor circinelloides | |
| Tartrate | inhibits at 10 mM | Mucor circinelloides | |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| cytosol | - |
Mortierella alpina | 5829 | - |
| cytosol | - |
Mucor circinelloides | 5829 | - |
| cytosol | - |
Escherichia coli | 5829 | - |
| cytosol | - |
Mucoromycotina sp. | 5829 | - |
| cytosol | - |
Rhodotorula toruloides | 5829 | - |
| cytosol | - |
Cunninghamella bainieri | 5829 | - |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Fe2+ | activates | Cunninghamella bainieri | |
| Mg2+ | dependent on | Cunninghamella bainieri | |
| additional information | a divalent metal ion is required as cofactor for the reaction | Mucor circinelloides | |
| additional information | a divalent metal ion is required as cofactor for the reaction | Mortierella alpina | |
| additional information | a divalent metal ion is required as cofactor for the reaction | Escherichia coli | |
| additional information | a divalent metal ion is required as cofactor for the reaction | Rhodotorula toruloides | |
| additional information | a divalent metal ion is required as cofactor for the reaction | Cunninghamella bainieri | |
| additional information | CoA has little effect on MaeB | Escherichia coli | |
| Zn2+ | activates | Cunninghamella bainieri | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| (S)-malate + NADP+ | Mortierella alpina | - |
pyruvate + CO2 + NADPH | - |
? | |
| (S)-malate + NADP+ | Mucor circinelloides | - |
pyruvate + CO2 + NADPH | - |
r | |
| (S)-malate + NADP+ | Mortierella alpina | - |
pyruvate + CO2 + NADPH | - |
r | |
| (S)-malate + NADP+ | Escherichia coli | - |
pyruvate + CO2 + NADPH | - |
r | |
| (S)-malate + NADP+ | Mucoromycotina sp. | - |
pyruvate + CO2 + NADPH | - |
? | |
| (S)-malate + NADP+ | Rhodotorula toruloides | - |
pyruvate + CO2 + NADPH | - |
r | |
| (S)-malate + NADP+ | Cunninghamella bainieri | - |
pyruvate + CO2 + NADPH | - |
r | |
| (S)-malate + NADP+ | Cunninghamella bainieri 2A1 | - |
pyruvate + CO2 + NADPH | - |
r | |
| (S)-malate + NADP+ | Mucor circinelloides CBS 108.16 | - |
pyruvate + CO2 + NADPH | - |
r | |
| (S)-malate + NADP+ | Rhodotorula toruloides CBS 14 | - |
pyruvate + CO2 + NADPH | - |
r | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Cunninghamella bainieri | - |
- |
- |
| Cunninghamella bainieri 2A1 | - |
- |
- |
| Escherichia coli | P76558 | - |
- |
| Mortierella alpina | - |
- |
- |
| Mortierella alpina | A6XP71 | - |
- |
| Mucor circinelloides | A6XP72 | at least six isoforms (I to VI) in strain CBS 108.16 | - |
| Mucor circinelloides CBS 108.16 | A6XP72 | at least six isoforms (I to VI) in strain CBS 108.16 | - |
| Mucoromycotina sp. | - |
- |
- |
| Rhodotorula toruloides | M7WHN9 | - |
- |
| Rhodotorula toruloides CBS 14 | M7WHN9 | - |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| (S)-malate + NADP+ | - |
Mortierella alpina | pyruvate + CO2 + NADPH | - |
? | |
| (S)-malate + NADP+ | - |
Mucor circinelloides | pyruvate + CO2 + NADPH | - |
r | |
| (S)-malate + NADP+ | - |
Mortierella alpina | pyruvate + CO2 + NADPH | - |
r | |
| (S)-malate + NADP+ | - |
Escherichia coli | pyruvate + CO2 + NADPH | - |
r | |
| (S)-malate + NADP+ | - |
Mucoromycotina sp. | pyruvate + CO2 + NADPH | - |
? | |
| (S)-malate + NADP+ | - |
Rhodotorula toruloides | pyruvate + CO2 + NADPH | - |
r | |
| (S)-malate + NADP+ | - |
Cunninghamella bainieri | pyruvate + CO2 + NADPH | - |
r | |
| (S)-malate + NADP+ | - |
Cunninghamella bainieri 2A1 | pyruvate + CO2 + NADPH | - |
r | |
| (S)-malate + NADP+ | - |
Mucor circinelloides CBS 108.16 | pyruvate + CO2 + NADPH | - |
r | |
| (S)-malate + NADP+ | - |
Rhodotorula toruloides CBS 14 | pyruvate + CO2 + NADPH | - |
r | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| MaeB | - |
Escherichia coli |
| malic enzyme | - |
Mucor circinelloides |
| malic enzyme | - |
Mortierella alpina |
| malic enzyme | - |
Escherichia coli |
| malic enzyme | - |
Rhodotorula toruloides |
| malic enzyme | - |
Cunninghamella bainieri |
| NADP+-ME | - |
Mortierella alpina |
| NADP+-ME | - |
Mucoromycotina sp. |
| NADP-ME | - |
Mucor circinelloides |
| NADP-ME | - |
Mortierella alpina |
| NADP-ME | - |
Escherichia coli |
| NADP-ME | - |
Rhodotorula toruloides |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| NADP+ | - |
Mortierella alpina | |
| NADP+ | - |
Mucor circinelloides | |
| NADP+ | - |
Escherichia coli | |
| NADP+ | - |
Mucoromycotina sp. | |
| NADP+ | - |
Rhodotorula toruloides | |
| NADP+ | - |
Cunninghamella bainieri | |
| NADPH | - |
Mucor circinelloides | |
| NADPH | - |
Mortierella alpina | |
| NADPH | - |
Escherichia coli | |
| NADPH | - |
Rhodotorula toruloides | |
| NADPH | - |
Cunninghamella bainieri | |
Expression
| Organism | Comment | Expression |
|---|---|---|
| Cunninghamella bainieri | ammonium tartrate as nitrogen source induces isozyme D | up |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | the enzyme belongs to the malic superfamily and the NAD_bind_amino_acid_DH superfamily which is a member of the Rossmann fold superfamily | Mucor circinelloides |
| evolution | the enzyme belongs to the malic superfamily and the NAD_bind_amino_acid_DH superfamily which is a member of the Rossmann fold superfamily | Mortierella alpina |
| evolution | the enzyme belongs to the malic superfamily and the NAD_bind_amino_acid_DH superfamily which is a member of the Rossmann fold superfamily | Escherichia coli |
| evolution | the enzyme belongs to the malic superfamily and the NAD_bind_amino_acid_DH superfamily which is a member of the Rossmann fold superfamily | Rhodotorula toruloides |
| malfunction | the decrease of malic enzyme activity is consistent with the cease of lipid accumulation. Reduction of malic enzyme activity is not due to the downregulation of malic enzyme but the feedback repression after nitrogen starvation. Malic enzyme activity recovered by adding ammonium tartrate even at a high cyclohexamide concentration | Cunninghamella bainieri |
| malfunction | the deprivation of malic enzyme activity limited the lipid accumulation | Mucor circinelloides |
| metabolism | the enzyme is involved in the transhydrogenase cycle, overview. In view of NADPH as the requisite reducing power in lipid production, the stability of malic enzyme is therefore crucial and malic enzyme activity is significant in the regulation of lipid accumulation | Mucor circinelloides |
| metabolism | the enzyme is involved in the transhydrogenase cycle, overview. In view of NADPH as the requisite reducing power in lipid production, the stability of malic enzyme is therefore crucial and malic enzyme activity is significant in the regulation of lipid accumulation | Mortierella alpina |
| metabolism | the enzyme is involved in the transhydrogenase cycle, overview. In view of NADPH as the requisite reducing power in lipid production, the stability of malic enzyme is therefore crucial and malic enzyme activity is significant in the regulation of lipid accumulation | Escherichia coli |
| metabolism | the enzyme is involved in the transhydrogenase cycle, overview. In view of NADPH as the requisite reducing power in lipid production, the stability of malic enzyme is therefore crucial and malic enzyme activity is significant in the regulation of lipid accumulation | Cunninghamella bainieri |
| metabolism | the enzyme is involved in the transhydrogenase cycle, overview. In view of NADPH as the requisite reducing power in lipid production, the stability of malic enzyme is therefore crucial and malic enzyme activity is significant in the regulation of lipid accumulation. The enzyme serves as the sole source of NADPH for fatty acid biosynthesis | Rhodotorula toruloides |
| physiological function | malic enzyme (ME) is a key enzyme regulating the lipid accumulation process in oleaginous microorganisms. It catalyzes the oxidative decarboxylation of L-malate to pyruvate and CO2 with concomitant reduction of NADP+ to NADPH, supplying the reducing power for fatty acid biosynthesis. The extent of lipid accumulation in some fungi is identified to be controlled by ME acting as the sole source of NADPH. Unique role of malic enzyme to provide NADPH for fatty acid synthesis as well as fatty acid desaturation | Mucor circinelloides |
| physiological function | malic enzyme (ME) is a key enzyme regulating the lipid accumulation process in oleaginous microorganisms. It catalyzes the oxidative decarboxylation of L-malate to pyruvate and CO2 with concomitant reduction of NADP+ to NADPH, supplying the reducing power for fatty acid biosynthesis. The extent of lipid accumulation in some fungi is identified to be controlled by ME acting as the sole source of NADPH. Unique role of malic enzyme to provide NADPH for fatty acid synthesis as well as fatty acid desaturation | Mortierella alpina |
| physiological function | malic enzyme (ME) is a key enzyme regulating the lipid accumulation process in oleaginous microorganisms. It catalyzes the oxidative decarboxylation of L-malate to pyruvate and CO2 with concomitant reduction of NADP+ to NADPH, supplying the reducing power for fatty acid biosynthesis. The extent of lipid accumulation in some fungi is identified to be controlled by ME acting as the sole source of NADPH. Unique role of malic enzyme to provide NADPH for fatty acid synthesis as well as fatty acid desaturation | Escherichia coli |
| physiological function | malic enzyme (ME) is a key enzyme regulating the lipid accumulation process in oleaginous microorganisms. It catalyzes the oxidative decarboxylation of L-malate to pyruvate and CO2 with concomitant reduction of NADP+ to NADPH, supplying the reducing power for fatty acid biosynthesis. The extent of lipid accumulation in some fungi is identified to be controlled by ME acting as the sole source of NADPH. Unique role of malic enzyme to provide NADPH for fatty acid synthesis as well as fatty acid desaturation. Activity of isoform E is intensely associated with the profiles and the level of lipid biosynthesis in N-limitation condition, while isoform D is reduced as lipid is produced. With ammonium tartrate as nitrogen source, activity of isoform D is pronounced, while isoform E is very low. Isoform E is the crucial regulator of lipid accumulation in strain 2A1 | Cunninghamella bainieri |
| physiological function | malic enzyme (ME) is a key enzyme regulating the lipid accumulation process in oleaginous microorganisms. It catalyzes the oxidative decarboxylation of L-malate to pyruvate and CO2 with concomitant reduction of NADP+ to NADPH, supplying the reducing power for fatty acid biosynthesis. The extent of lipid accumulation in some fungi is identified to be controlled by ME acting as the sole source of NADPH. Unique role of malic enzyme to provide NADPH for fatty acid synthesis as well as fatty acid desaturation. The final governance over the malic enzyme activity is supposed to be the supply of its substrate | Rhodotorula toruloides |
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