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(2S,3R)-3-Hydroxybutane-1,2,3-tricarboxylate
?
(2S,3R)-3-Hydroxybutane-1,2,3-tricarboxylate
Pyruvate + succinate
(2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate
succinate + pyruvate
2-methylisocitrate
succinate + pyruvate
2-methylisocitrate lactone
succinate + pyruvate
methylisocitrate
succinate + pyruvate
additional information
?
-
(2S,3R)-3-Hydroxybutane-1,2,3-tricarboxylate
?
-
enzyme of propionate catabolism
-
-
?
(2S,3R)-3-Hydroxybutane-1,2,3-tricarboxylate
?
-
enzyme of propionate catabolism
-
-
?
(2S,3R)-3-Hydroxybutane-1,2,3-tricarboxylate
?
-
enzyme of propionate catabolism
-
-
?
(2S,3R)-3-Hydroxybutane-1,2,3-tricarboxylate
?
-
enzyme of propionate catabolism
-
-
?
(2S,3R)-3-Hydroxybutane-1,2,3-tricarboxylate
?
-
enzyme of propionate catabolism
-
-
?
(2S,3R)-3-Hydroxybutane-1,2,3-tricarboxylate
?
-
enzyme of propionate catabolism
-
-
?
(2S,3R)-3-Hydroxybutane-1,2,3-tricarboxylate
?
-
enzyme of propionate catabolism
-
-
?
(2S,3R)-3-Hydroxybutane-1,2,3-tricarboxylate
?
-
enzyme of propionate catabolism
-
-
?
(2S,3R)-3-Hydroxybutane-1,2,3-tricarboxylate
?
-
enzyme of propionate catabolism
-
-
?
(2S,3R)-3-Hydroxybutane-1,2,3-tricarboxylate
?
Ustilago crus-galli
-
enzyme of propionate catabolism
-
-
?
(2S,3R)-3-Hydroxybutane-1,2,3-tricarboxylate
?
Ustilago crus-galli F-B-6
-
enzyme of propionate catabolism
-
-
?
(2S,3R)-3-Hydroxybutane-1,2,3-tricarboxylate
?
Ustilago utriculosa
-
enzyme of propionate catabolism
-
-
?
(2S,3R)-3-Hydroxybutane-1,2,3-tricarboxylate
?
Ustilago utriculosa F-B-5
-
enzyme of propionate catabolism
-
-
?
(2S,3R)-3-Hydroxybutane-1,2,3-tricarboxylate
?
-
enzyme of propionate catabolism
-
-
?
(2S,3R)-3-Hydroxybutane-1,2,3-tricarboxylate
?
-
enzyme of propionate catabolism
-
-
?
(2S,3R)-3-Hydroxybutane-1,2,3-tricarboxylate
?
-
enzyme synthesis is repressed by glucose
-
-
?
(2S,3R)-3-Hydroxybutane-1,2,3-tricarboxylate
?
-
key enzyme in propionate metabolism
-
-
?
(2S,3R)-3-Hydroxybutane-1,2,3-tricarboxylate
?
-
the enzyme may function to supply pyruvate, the end-product of the catabolism of the propionate residue, to various reactions
-
-
?
(2S,3R)-3-Hydroxybutane-1,2,3-tricarboxylate
?
-
regulatory enzyme of the methylcitric acid cycle
-
-
?
(2S,3R)-3-Hydroxybutane-1,2,3-tricarboxylate
Pyruvate + succinate
-
syn: methylisocitrate, enzyme acts only on threo-diastereomer, but not on the erythro-diastereomer
-
?
(2S,3R)-3-Hydroxybutane-1,2,3-tricarboxylate
Pyruvate + succinate
-
one of the key enzymes of the methylcitrate cycle. Deletion mutants do not grow on propionate as sole carbon and energy source and are severely inhibited during growth on alternative carbon sources, when propionate is present. The strongest inhibitory effect is observed, when glycerol is the main carbon source, followed by glucose and acetate. In addition, asexual conidiation is strongly impaired in the presence of propionate
-
-
?
(2S,3R)-3-Hydroxybutane-1,2,3-tricarboxylate
Pyruvate + succinate
-
the enzyme is highly specific for (2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate
-
-
?
(2S,3R)-3-Hydroxybutane-1,2,3-tricarboxylate
Pyruvate + succinate
syn: methylisocitrate
-
?
(2S,3R)-3-Hydroxybutane-1,2,3-tricarboxylate
Pyruvate + succinate
a catalytic mechanism is proposed that involves an R-carboxy-carbanion intermediate/transition state, which is consistent with previous stereochemical experiments showing inversion of configuration at the C(3) of 2-methyl-isocitrate
-
-
?
(2S,3R)-3-Hydroxybutane-1,2,3-tricarboxylate
Pyruvate + succinate
-
-
-
-
?
(2S,3R)-3-Hydroxybutane-1,2,3-tricarboxylate
Pyruvate + succinate
-
-
-
-
?
(2S,3R)-3-Hydroxybutane-1,2,3-tricarboxylate
Pyruvate + succinate
-
-
-
-
?
(2S,3R)-3-Hydroxybutane-1,2,3-tricarboxylate
Pyruvate + succinate
-
syn: methylisocitrate
-
?
(2S,3R)-3-Hydroxybutane-1,2,3-tricarboxylate
Pyruvate + succinate
-
-
-
?
(2S,3R)-3-Hydroxybutane-1,2,3-tricarboxylate
Pyruvate + succinate
-
-
-
?
(2S,3R)-3-Hydroxybutane-1,2,3-tricarboxylate
Pyruvate + succinate
-
reverse reaction not detected
-
?
(2S,3R)-3-Hydroxybutane-1,2,3-tricarboxylate
Pyruvate + succinate
-
specific for threo-DS-2-methylisocitrate
-
?
(2S,3R)-3-Hydroxybutane-1,2,3-tricarboxylate
Pyruvate + succinate
-
no activity with 2R,3S-isocitrate
-
?
(2S,3R)-3-Hydroxybutane-1,2,3-tricarboxylate
Pyruvate + succinate
-
i.e. 2-methylisocitrate, , threo-DS-2-methylisocitrate
-
?
(2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate
succinate + pyruvate
-
-
-
-
?
(2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate
succinate + pyruvate
-
-
-
-
?
(2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate
succinate + pyruvate
-
-
-
-
?
(2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate
succinate + pyruvate
-
-
-
-
?
(2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate
succinate + pyruvate
-
-
-
-
?
2-methylisocitrate
succinate + pyruvate
-
-
-
?
2-methylisocitrate
succinate + pyruvate
the enzyme is involved in the methylcitric acid cycle
-
-
?
2-methylisocitrate
succinate + pyruvate
-
-
-
?
2-methylisocitrate
succinate + pyruvate
the enzyme is involved in the methylcitric acid cycle
-
-
?
2-methylisocitrate lactone
succinate + pyruvate
-
-
-
-
?
2-methylisocitrate lactone
succinate + pyruvate
-
-
-
-
?
methylisocitrate
succinate + pyruvate
-
-
-
-
?
methylisocitrate
succinate + pyruvate
-
-
-
-
?
additional information
?
-
-
no substrate: isocitrate
-
?
additional information
?
-
-
enzyme in methylcitrate cycle
-
?
additional information
?
-
enzyme in methylcitrate cycle
-
?
additional information
?
-
-
enzyme in methylcitrate cycle
-
?
additional information
?
-
-
Mycobacterium tuberculosis isocitrate lyases are catalytically bifunctional isocitrate and methylisocitrate lyases, EC 4.1.3.1 and EC 4.1.3.30, required for growth on even and odd chain fatty acids
-
-
?
additional information
?
-
-
enzyme in methylcitrate cycle
-
?
additional information
?
-
-
no substrate: isocitrate
-
?
additional information
?
-
-
enzyme in methylcitrate cycle
-
?
additional information
?
-
-
enzyme in methylcitrate cycle
-
?
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(2S,3R)-3-Hydroxybutane-1,2,3-tricarboxylate
?
(2S,3R)-3-Hydroxybutane-1,2,3-tricarboxylate
Pyruvate + succinate
-
one of the key enzymes of the methylcitrate cycle. Deletion mutants do not grow on propionate as sole carbon and energy source and are severely inhibited during growth on alternative carbon sources, when propionate is present. The strongest inhibitory effect is observed, when glycerol is the main carbon source, followed by glucose and acetate. In addition, asexual conidiation is strongly impaired in the presence of propionate
-
-
?
(2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate
succinate + pyruvate
2-methylisocitrate
succinate + pyruvate
additional information
?
-
(2S,3R)-3-Hydroxybutane-1,2,3-tricarboxylate
?
-
enzyme of propionate catabolism
-
-
?
(2S,3R)-3-Hydroxybutane-1,2,3-tricarboxylate
?
-
enzyme of propionate catabolism
-
-
?
(2S,3R)-3-Hydroxybutane-1,2,3-tricarboxylate
?
-
enzyme of propionate catabolism
-
-
?
(2S,3R)-3-Hydroxybutane-1,2,3-tricarboxylate
?
-
enzyme of propionate catabolism
-
-
?
(2S,3R)-3-Hydroxybutane-1,2,3-tricarboxylate
?
-
enzyme of propionate catabolism
-
-
?
(2S,3R)-3-Hydroxybutane-1,2,3-tricarboxylate
?
-
enzyme of propionate catabolism
-
-
?
(2S,3R)-3-Hydroxybutane-1,2,3-tricarboxylate
?
-
enzyme of propionate catabolism
-
-
?
(2S,3R)-3-Hydroxybutane-1,2,3-tricarboxylate
?
-
enzyme of propionate catabolism
-
-
?
(2S,3R)-3-Hydroxybutane-1,2,3-tricarboxylate
?
-
enzyme of propionate catabolism
-
-
?
(2S,3R)-3-Hydroxybutane-1,2,3-tricarboxylate
?
Ustilago crus-galli
-
enzyme of propionate catabolism
-
-
?
(2S,3R)-3-Hydroxybutane-1,2,3-tricarboxylate
?
Ustilago crus-galli F-B-6
-
enzyme of propionate catabolism
-
-
?
(2S,3R)-3-Hydroxybutane-1,2,3-tricarboxylate
?
Ustilago utriculosa
-
enzyme of propionate catabolism
-
-
?
(2S,3R)-3-Hydroxybutane-1,2,3-tricarboxylate
?
Ustilago utriculosa F-B-5
-
enzyme of propionate catabolism
-
-
?
(2S,3R)-3-Hydroxybutane-1,2,3-tricarboxylate
?
-
enzyme of propionate catabolism
-
-
?
(2S,3R)-3-Hydroxybutane-1,2,3-tricarboxylate
?
-
enzyme of propionate catabolism
-
-
?
(2S,3R)-3-Hydroxybutane-1,2,3-tricarboxylate
?
-
enzyme synthesis is repressed by glucose
-
-
?
(2S,3R)-3-Hydroxybutane-1,2,3-tricarboxylate
?
-
key enzyme in propionate metabolism
-
-
?
(2S,3R)-3-Hydroxybutane-1,2,3-tricarboxylate
?
-
the enzyme may function to supply pyruvate, the end-product of the catabolism of the propionate residue, to various reactions
-
-
?
(2S,3R)-3-Hydroxybutane-1,2,3-tricarboxylate
?
-
regulatory enzyme of the methylcitric acid cycle
-
-
?
(2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate
succinate + pyruvate
-
-
-
-
?
(2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate
succinate + pyruvate
-
-
-
-
?
(2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate
succinate + pyruvate
-
-
-
-
?
(2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate
succinate + pyruvate
-
-
-
-
?
(2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate
succinate + pyruvate
-
-
-
-
?
2-methylisocitrate
succinate + pyruvate
the enzyme is involved in the methylcitric acid cycle
-
-
?
2-methylisocitrate
succinate + pyruvate
the enzyme is involved in the methylcitric acid cycle
-
-
?
additional information
?
-
-
enzyme in methylcitrate cycle
-
?
additional information
?
-
enzyme in methylcitrate cycle
-
?
additional information
?
-
-
enzyme in methylcitrate cycle
-
?
additional information
?
-
-
Mycobacterium tuberculosis isocitrate lyases are catalytically bifunctional isocitrate and methylisocitrate lyases, EC 4.1.3.1 and EC 4.1.3.30, required for growth on even and odd chain fatty acids
-
-
?
additional information
?
-
-
enzyme in methylcitrate cycle
-
?
additional information
?
-
-
enzyme in methylcitrate cycle
-
?
additional information
?
-
-
enzyme in methylcitrate cycle
-
?
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(4E)-4-[(4,7-dichloro-2-phenyl-1H-indol-3-yl)methylidene]-2,4-dihydro-3H-pyrazol-3-one
-
-
(4E)-4-[(5-methyl-2-phenyl-1H-indol-3-yl)methylidene]-2,4-dihydro-3H-pyrazol-3-one
-
-
(4E)-4-[(6,7-dichloro-2-phenyl-1H-indol-3-yl)methylidene]-2,4-dihydro-3H-pyrazol-3-one
-
-
(4Z)-5-methyl-4-[(1H-pyrrol-2-yl)methylidene]-2,4-dihydro-3H-pyrazol-3-one
-
-
(4Z)-5-methyl-4-[(pyridin-4-yl)methylidene]-2,4-dihydro-3H-pyrazol-3-one
-
-
3-(4,7-dichloro-2-phenyl-1H-indol-3-yl)-4-methyl-3a,6-dihydropyrazolo[3,4-c]pyrazole-2(3H)-carbothioamide
-
-
3-(6,7-dichloro-2-phenyl-1H-indol-3-yl)-4-methyl-3a,6-dihydropyrazolo[3,4-c]pyrazole-2(3H)-carbothioamide
-
-
3-(6,7-dichloro-2-phenyl-1H-indol-3-yl)-4-methyl-3a,6-dihydropyrazolo[3,4-c]pyrazole-2(3H)-carboxamide
-
-
3-Bromopyruvate
-
complete inactivation at equimolar concentrations
4-methyl-3-(1H-pyrrol-2-yl)-3a,6-dihydropyrazolo[3,4-c]pyrazole-2(3H)-carboxamide
-
-
4-methyl-3-(5-methyl-2-phenyl-1H-indol-3-yl)-3a,6-dihydropyrazolo[3,4-c]pyrazole-2(3H)-carbothioamide
-
-
4-methyl-3-(5-methyl-2-phenyl-1H-indol-3-yl)-3a,6-dihydropyrazolo[3,4-c]pyrazole-2(3H)-carboxamide
-
-
4-methyl-3-(pyridin-4-yl)-3a,6-dihydropyrazolo[3,4-c]pyrazole-2(3H)-carbothioamide
-
-
4-methyl-3-(pyridin-4-yl)-3a,6-dihydropyrazolo[3,4-c]pyrazole-2(3H)-carboxamide
-
-
6,7-dichloro-3-(4-methyl-2-phenyl-2,3,3a,6-tetrahydropyrazolo[3,4-c]pyrazol-3-yl)-2-phenyl-1H-indole
-
-
Ca2+
-
40% inactivation at 2 mM; inhibition at 2 mM
Cu2+
-
10 mM, in presence of 2.5 mM Mg2+, 10% inhibition
Hg2+
-
10 mM, in presence of 2.5 mM Mg2+, 30% inhibition
Itaconic acid
-
itaconic acid specifically inhibits growth of wild-type cells on acetate and propionate, but not dextrose, in an ICL-dependent manner, and elicited metabolomic changes similar to those observed with ICL-deficient cells. Enzyme ICL inhibition by itaconic acid results in a specific decrease in intrabacterial pH from pH 7.3 to pH 6.4 in propionat-grown cells, not in acetate-grown cells
p-chloromercuribenzoate
-
-
Pb2+
-
10 mM, in presence of 2.5 mM Mg2+, 14% inhibition. 11% activation, when added instead of Mg2+
Zn2+
-
10 mM, in presence of 2.5 mM Mg2+, 34% inhibition
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0.024 - 57
(2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate
0.0181 - 0.0806
methylisocitrate
0.024
(2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate
-
0.77
(2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate
-
-
10
(2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate
-
pH 7.5, 37°C, H125A mutant
19
(2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate
-
pH 7
19
(2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate
-
pH 7.5, 37°C, wild-type
22
(2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate
-
pH 7.5, 37°C, R122K mutant
31
(2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate
-
pH 7
57
(2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate
-
pH 7.5, 37°C, K121A mutant
0.0181
methylisocitrate
-
wild type protein, pH not specified in the publication, temperature not specified in the publication
0.0485
methylisocitrate
-
L521F/S523T mutant protein, pH not specified in the publication, temperature not specified in the publication
0.0674
methylisocitrate
-
S523T mutant protein, pH not specified in the publication, temperature not specified in the publication
0.0806
methylisocitrate
-
L521F mutant protein, pH not specified in the publication, temperature not specified in the publication
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evolution
the 2-methylcitrate cycle enzymes have been acquired via horizontal gene transfer, PrpB phylogenetic analysis, overview
malfunction
-
the DELTAMCL1 strains fail to grow on propionate but exhibit no major changes in other traits, double deletion of both isocitrate lyase 1 and methylisocitrate lyase 1 cause significantly reduced virulence on host plants
malfunction
-
a plate confrontation assay does not show a difference between the wild-type and the DELTAmcl deletion strain in antagonism towards Botrytis cinerea. But the DELTAmcl strain displays reduced antagonism towards Botrytis cinerea based on a secretion assay. An in vitro root colonization assay shows that the DELTAmcl strain has reduced ability to colonize Arabidopsis thaliana roots, which results in reduced induction of systemic resistance towards Botrytis cinerea. phenotype, overview. The DELTAmcl strain showed significantly reduced numbers of germinating conidia and delayed conidial pigmentation, as well as decreased tolerance to osmotic stress
malfunction
-
absence of MCL activity results in the accumulation of methylisocitrate as a metabolic dead end product arising from the stoichiometric consumption of oxaloacetate by propionyl-CoA, phenotype, overview. Isocitrate lyases are essential for survival on both acetate and propionate because of its methylisocitrate lyase activity. Lack of methylisocitrate lyase activity converts the cell methylcitrate cycle into a dead end pathway that sequesters tricarboxylic acid (TCA) cycle intermediates into methylcitrate cycle intermediates, depletes gluconeogenic precursors, and results in defects of membrane potential and intrabacterial pH
malfunction
an enzyme-disruption mutant prpb-ko shows accumulation of 2-methylcitrate cycle intermediate metabolites, enzyme substrates accumulate in parasites deficient in the enzyme and its absence confers increased sensitivity to propionic acid
malfunction
-
the DELTAMCL1 strains fail to grow on propionate but exhibit no major changes in other traits, double deletion of both isocitrate lyase 1 and methylisocitrate lyase 1 cause significantly reduced virulence on host plants
-
malfunction
-
a plate confrontation assay does not show a difference between the wild-type and the DELTAmcl deletion strain in antagonism towards Botrytis cinerea. But the DELTAmcl strain displays reduced antagonism towards Botrytis cinerea based on a secretion assay. An in vitro root colonization assay shows that the DELTAmcl strain has reduced ability to colonize Arabidopsis thaliana roots, which results in reduced induction of systemic resistance towards Botrytis cinerea. phenotype, overview. The DELTAmcl strain showed significantly reduced numbers of germinating conidia and delayed conidial pigmentation, as well as decreased tolerance to osmotic stress
-
metabolism
-
role of the methylcitrate cycle in propionate metabolism
metabolism
the enzyme is involved in the methylcitric acid cycle
metabolism
-
the enzyme is involved in the methylcitric acid cycle
-
metabolism
-
role of the methylcitrate cycle in propionate metabolism
-
physiological function
-
MCL1 is required for the methylcitrate cycle in Gibberella zeae
physiological function
-
methylisocitrate lyase is a signature enzyme of the methylcitrate cycle, which is required for propionate metabolism, for secondary metabolite production and for virulence in bacteria and fungi. The enzyme is required in propionate resistance, growth, conidial pigmentation and germination, and abiotic stress tolerance
physiological function
-
Mycobacterium tuberculosis isocitrate lyases are catalytically bifunctional isocitrate and methylisocitrate lyases required for growth on even and odd chain fatty acids
physiological function
the enzyme is involved in the 2-methylcitrate cycle required to metabolize and detoxify propionate by oxidation to pyruvate, but the rate-limiting enzyme 2-methylisocitrate lyase is dispensable for parasite survival
physiological function
-
the enzyme is essential for the survival of Pseudomonas aeruginosa
physiological function
-
MCL1 is required for the methylcitrate cycle in Gibberella zeae
-
physiological function
-
methylisocitrate lyase is a signature enzyme of the methylcitrate cycle, which is required for propionate metabolism, for secondary metabolite production and for virulence in bacteria and fungi. The enzyme is required in propionate resistance, growth, conidial pigmentation and germination, and abiotic stress tolerance
-
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Uchiyama, H.; Ando, M.; Toyonaka, Y.; Tabuchi, T.
Subcellular localization of the methylcitric-acid-cycle enzymes in propionate metabolism of Yarrowia lipolytica
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Yarrowia lipolytica
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Tabuchi, T.; Igoshi, K.
Regulation of enzyme synthesis of the glycolate, the citric acid, and the methylcitric acid cycles in Candida lipolytica
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Yarrowia lipolytica
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Tabuchi, T.; Satoh, T.
Purification and properties of methylisocitrate lyase, a key enzyme in propionate metabolism, from Candida lipolytica
Agric. Biol. Chem.
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Yarrowia lipolytica
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Tabuchi, T.; Satoh, T.
Distinction between isocitrate lyase and methylisocitrate lyase in Candida lipolytica
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Yarrowia lipolytica
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Miyakoshi, S.; Uchiyama, H.; Someya, T.; Satoh, T.; Tabuchi, T.
Distribution of the methylcitric acid cycle and beta-oxidation pathway for propionate catabolism in fungi
Agric. Biol. Chem.
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Aspergillus niger, Wickerhamiella pararugosa, Diutina rugosa, Mucor rouxianus, Neurospora crassa, Rhizopus microsporus var. chinensis, Ustilago crus-galli, Ustilago utriculosa, Rhizopus microsporus var. chinensis IAM 6003, Neurospora crassa IFO 6067, Mucor rouxianus IFO 5773, Ustilago utriculosa F-B-5, Diutina rugosa IFO 0750, Wickerhamiella pararugosa IFO 0966, Ustilago crus-galli F-B-6
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Simanshu, D.K.; Satheshkumar, P.S.; Savithri, H.S.; Murthy, M.R.
Crystal structure of Salmonella typhimurium 2-methylisocitrate lyase (PrpB) and its complex with pyruvate and Mg(2+)
Biochem. Biophys. Res. Commun.
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2003
Salmonella enterica subsp. enterica serovar Typhimurium
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Brock, M.; Darley, D.; Textor, S.; Buckel, W.
2-Methylisocitrate lyases from the bacterium Escherichia coli and the filamentous fungus Aspergillus nidulans: characterization and comparison of both enzymes
Eur. J. Biochem.
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Aspergillus nidulans
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Luttik, M.A.; Kotter, P.; Salomons, F.A.; van der Klei, I.J.; van Dijken, J.P.; Pronk, J.T.
The Saccharomyces cerevisiae ICL2 gene encodes a mitochondrial 2-methylisocitrate lyase involved in propionyl-coenzyme A metabolism
J. Bacteriol.
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Saccharomyces cerevisiae
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Grimek, T.L.; Holden, H.; Rayment, I.; Escalante-Semerena, J.C.
Residues C123 and D58 of the 2-methylisocitrate lyase (PrpB) enzyme of Salmonella enterica are essential for catalysis
J. Bacteriol.
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4837-4843
2003
Salmonella enterica
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Grimm, C.; Evers, A.; Brock, M.; Maerker, C.; Klebe, G.; Buckel, W.; Reuter, K.
Crystal structure of 2-methylisocitrate lyase (PrpB) from Escherichia coli and modelling of its ligand bound active centre
J. Mol. Biol.
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2003
Escherichia coli (P77541), Escherichia coli
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Brock, M.
Generation and phenotypic characterization of Aspergillus nidulans methylisocitrate lyase deletion mutants: methylisocitrate inhibits growth and conidiation
Appl. Environ. Microbiol.
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5465-5475
2005
Aspergillus nidulans
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Liu, S.; Lu, Z.; Han, Y.; Melamud, E.; Dunaway-Mariano, D.; Herzberg, O.
Crystal structures of 2-methylisocitrate lyase in complex with product and with isocitrate inhibitor provide insight into lyase substrate specificity, catalysis and evolution
Biochemistry
44
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2005
Escherichia coli (P77541)
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Upton, A.M.; McKinney, J.D.
Role of the methylcitrate cycle in propionate metabolism and detoxification in Mycobacterium smegmatis
Microbiology
153
3973-3982
2007
Mycolicibacterium smegmatis, Mycolicibacterium smegmatis mc(2)155 / ATCC 700084
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Munoz-Elias, E.J.; Upton, A.M.; Cherian, J.; McKinney, J.D.
Role of the methylcitrate cycle in Mycobacterium tuberculosis metabolism, intracellular growth, and virulence
Mol. Microbiol.
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2006
Mycobacterium tuberculosis
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Gould, T.A.; van de Langemheen, H.; Munoz-Elias, E.J.; McKinney, J.D.; Sacchettini, J.C.
Dual role of isocitrate lyase 1 in the glyoxylate and methylcitrate cycles in Mycobacterium tuberculosis
Mol. Microbiol.
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940-947
2006
Mycobacterium tuberculosis
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Lee, S.H.; Han, Y.K.; Yun, S.H.; Lee, Y.W.
Roles of the glyoxylate and methylcitrate cycles in sexual development and virulence in the cereal pathogen Gibberella zeae
Eukaryot. Cell
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2009
Fusarium graminearum, Fusarium graminearum Z03643
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Mueller, S.; Fleck, C.B.; Wilson, D.; Hummert, C.; Hube, B.; Brock, M.
Gene acquisition, duplication and metabolic specification: the evolution of fungal methylisocitrate lyases
Environ. Microbiol.
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2011
Aspergillus fumigatus, Aspergillus fumigatus Af293
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Dubey, M.K.; Broberg, A.; Jensen, D.F.; Karlsson, M.
Role of the methylcitrate cycle in growth, antagonism and induction of systemic defence responses in the fungal biocontrol agent Trichoderma atroviride
Microbiology
159
2492-2500
2013
Trichoderma atroviride, Trichoderma atroviride IMI206040
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Limenitakis, J.; Oppenheim, R.D.; Creek, D.J.; Foth, B.J.; Barrett, M.P.; Soldati-Favre, D.
The 2-methylcitrate cycle is implicated in the detoxification of propionate in Toxoplasma gondii
Mol. Microbiol.
87
894-908
2013
Toxoplasma gondii (Q2L8W6), Toxoplasma gondii
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Eoh, H.; Rhee, K.Y.
Methylcitrate cycle defines the bactericidal essentiality of isocitrate lyase for survival of Mycobacterium tuberculosis on fatty acids
Proc. Natl. Acad. Sci. USA
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4976-4981
2014
Mycobacterium tuberculosis
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Reddick, J.J.; Sirkisoon, S.; Dahal, R.A.; Hardesty, G.; Hage, N.E.; Booth, W.T.; Quattlebaum, A.L.; Mills, S.N.; Meadows, V.G.; Adams, S.L.H.; Doyle, J.S.; Kiel, B.E.
First biochemical characterization of a methylcitric acid cycle from Bacillus subtilis strain 168
Biochemistry
56
5698-5711
2017
Bacillus subtilis (P54528), Bacillus subtilis 168 (P54528)
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Pulaganti, M.; C M, A.; Kumar, C.S.
Design, synthesis, and evaluation of pyrazolo-pyrazole derivatives on methylisocitrate lyase of Pseudomonas aeruginosa in silico and in vitro study
J. Biomol. Struct. Dyn.
35
2509-2529
2017
Pseudomonas aeruginosa
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Jongkon, N.; Chotpatiwetchkul, W.; Gleeson, M.P.
Probing the catalytic mechanism involved in the isocitrate lyase superfamily hybrid quantum mechanical/molecular mechanical calculations on 2,3-dimethylmalate lyase
J. Phys. Chem. B
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11473-11484
2015
Mycobacterium tuberculosis
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Lee, J.J.; Lim, J.; Gao, S.; Lawson, C.P.; Odell, M.; Raheem, S.; Woo, J.; Kang, S.H.; Kang, S.S.; Jeon, B.Y.; Eoh, H.
Glutamate mediated metabolic neutralization mitigates propionate toxicity in intracellular Mycobacterium tuberculosis
Sci. Rep.
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8506
2018
Mycobacterium tuberculosis, Mycobacterium tuberculosis BCG
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