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Information on EC 4.1.1.71 - 2-oxoglutarate decarboxylase for references in articles please use BRENDA:EC4.1.1.71Word Map on EC 4.1.1.71
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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
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2-oxoglutarate decarboxylase
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2-oxoglutarate = succinate semialdehyde + CO2
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TCA cycle IV (2-oxoglutarate decarboxylase)
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2-oxoglutarate carboxy-lyase (succinate-semialdehyde-forming)
Requires thiamine diphosphate. Highly specific.
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alpha-ketoglutarate decarboxylase
alpha-ketoglutaric decarboxylase
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decarboxylase, oxoglutarate
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Fe(II)/2OG-dependent decarboxylase
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oxoglutarate decarboxylase
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pre-2-oxoglutarate decarboxylase
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alpha-ketoglutarate decarboxylase
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alpha-ketoglutarate decarboxylase
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alpha-ketoglutarate decarboxylase
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alpha-ketoglutarate decarboxylase
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alpha-ketoglutarate decarboxylase
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alpha-ketoglutarate decarboxylase
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Kgd
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UniProt
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B 211
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B 211
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lacking a 2-oxoglutarate dehydrogenase complex (EC 1.2.4.2 + EC 2.3.1.61 + EC 1.8.1.4)
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UniProt
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UniProt
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2-oxoglutarate
succinate semialdehyde + CO2
additional information
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2-oxoglutarate
succinate semialdehyde + CO2
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2-oxoglutarate
succinate semialdehyde + CO2
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2-oxoglutarate
succinate semialdehyde + CO2
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highly specific
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2-oxoglutarate
succinate semialdehyde + CO2
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highly specific
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2-oxoglutarate
succinate semialdehyde + CO2
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2-oxoglutarate
succinate semialdehyde + CO2
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2-oxoglutarate
succinate semialdehyde + CO2
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2-oxoglutarate
succinate semialdehyde + CO2
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2-oxoglutarate
succinate semialdehyde + CO2
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2-oxoglutarate
succinate semialdehyde + CO2
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2-oxoglutarate
succinate semialdehyde + CO2
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2-oxoglutarate
succinate semialdehyde + CO2
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2-oxoglutarate
succinate semialdehyde + CO2
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oxaloacetate
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28% of the activity with 2-oxoglutarate
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oxaloacetate
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28% of the activity with 2-oxoglutarate
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additional information
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the enzyme has a physiologically important role coupling with succinate-semialdehyde dehydrogenase in the tricarboxylic acid cycle
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additional information
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enzyme has physiological function in the assimilation of L-glutamate
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additional information
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enzyme has physiological function in the assimilation of L-glutamate
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additional information
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enzyme and GabD1 or GabD2 form an alternative pathway from 2-oxoglutarate to succinate
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additional information
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no substrate: pyruvate
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additional information
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the 2-oxoglutarate dehydrogenase complex: 2-oxoglutarate decarboxylase and lipoamide dehydrogenase is a rate-limiting mitochondrial enzyme of the tricarboxylic acid cycle
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2-oxoglutarate
succinate semialdehyde + CO2
additional information
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2-oxoglutarate
succinate semialdehyde + CO2
A0R2B1
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2-oxoglutarate
succinate semialdehyde + CO2
A0R3B1
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2-oxoglutarate
succinate semialdehyde + CO2
A0R2B1
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2-oxoglutarate
succinate semialdehyde + CO2
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2-oxoglutarate
succinate semialdehyde + CO2
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additional information
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the enzyme has a physiologically important role coupling with succinate-semialdehyde dehydrogenase in the tricarboxylic acid cycle
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additional information
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enzyme has physiological function in the assimilation of L-glutamate
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additional information
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enzyme has physiological function in the assimilation of L-glutamate
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additional information
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enzyme and GabD1 or GabD2 form an alternative pathway from 2-oxoglutarate to succinate
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additional information
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the 2-oxoglutarate dehydrogenase complex: 2-oxoglutarate decarboxylase and lipoamide dehydrogenase is a rate-limiting mitochondrial enzyme of the tricarboxylic acid cycle
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additional information
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no cofactor: coenzyme A, NAD+, NADP+
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thiamine diphosphate
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Km: 0.056 mM; required
thiamine diphosphate
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0.03 mM; required
thiamine diphosphate
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Km-value 0.019 mM
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Mg2+
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strictly required, Km-value 0.196 mM
Ca2+
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can partially replace Mg2+ in activation
Co2+
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can partially replace Mg2+ in activation
MgCl2
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required
MgCl2
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Km: 0.093 mM; stimulates
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2-oxoglutarate
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above 2 mM substrate inhibition
m-chlorophenylhydrazone
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NH4Cl
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preferential sensitivity of enzyme to NH4Cl in vitro in nonsynaptic mitochondria and hyperammonemic conditions in vivo in synaptic mitochondria
Succinic semialdehyde
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additional information
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not: NaN3
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1,10-phenanthroline
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Cu2+
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Hg2+
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Zn2+
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L-glutamate
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activation is abolished by the simultaneous addition of cycloheximide
thiamine
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the activation of enzyme by thiamine is caused by two mechanism, the increase in the apoenzyme of enzyme by thiamine added exogenously is attributable to the conversion from the premature form to the mature form of enzyme during import into the mitochondria from cytosol, 1,10-phenanthroline, 2,4-dinitrophenol, carbonyl cyanide m-chlorophenylhydrazone inhibit activation
2-mercaptoethanol
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stimulates
2-mercaptoethanol
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stimulates
DTT
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stimulates
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additional information
additional information
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comparison of the effect of NH4Cl in vitro, hepatic encephalopathy, and hyperammonemia on KM in synaptic and nonsynaptic brain mitochondria
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0.33
2-oxoglutarate
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pH 7.0, 30°C
0.33
2-oxoglutarate
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pH 7.0
0.48
2-oxoglutarate
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22°C, pH 7.0
1
2-oxoglutarate
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pH 5.3, 30°C
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4 - 6.5
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active in the range
6 - 9
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pH 6.0: 65% of activity maximum, pH 9.0: 55% of activity maximum
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35 - 40
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35-40°C: activity maximum, maximum activity is maintained up to 60°C
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4.2
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isoelectric focusing
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additional information
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not: cytosol, microsomes
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exclusively
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synaptic and nonsynaptic
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Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155);
A0R2B1
Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155);
A0R2B1
Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155);
A0R2B1
Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155);
A0R2B1
Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155);
A0R2B1
Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155);
A0R2B1
Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155);
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62000
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4 * 62000, SDS-PAGE
65000
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1 * 65000, SDS-PAGE
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tetramer
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4 * 62000, SDS-PAGE
homodimer
x-ray crystallography
homodimer
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x-ray crystallography
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homodimer
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x-ray crystallography
homodimer
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x-ray crystallography
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monomer
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1 * 65000, SDS-PAGE
monomer
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1 * 65000, SDS-PAGE
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hanging drop vapor diffusion method, using 39-46.5% (w/v) 2-methyl-2,4-pentanediol, 100 mM HEPES (pH 7.0), 200 mM NaCl
hanging drop vapor diffusion method, using 52-59% (w/v) 2-methyl-2,4-pentanediol and 22-25 mM sodium acetate
hanging drop vapor diffusion method, using 39-46.5% (w/v) 2-methyl-2,4-pentanediol, 100 mM HEPES (pH 7.0), 200 mM NaCl
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6.2 - 8.5
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62°C, 10 min, stable
648365
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57.5
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10 min, stable up to
60
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pH 5.3, 30 min, 10% loss of activity
62
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pH 6.2-8.5, 10 min, stable
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10 min, complete loss of activity
70
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complete loss of activity at 70°C
70
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pH 5.3, 5 min, 90% loss of activity
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the isolated proteins (ALKBH4 and mutants), even when kept in iced-cooled solutions (4°C), aggregate and then precipitate at concentrations higher than 0.5 mM. The process is accelerated greatly when an excess (e.g. 5fold) of dithionite is added to the solution when anaerobic Fe(II)-reconstitution procedures are carried out
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4°C or -20°C, 24 h, 95% or 25% loss of activity, respectively
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glutathione-Sepharose column chromatography, gel filtration
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HisTrap column chromatography and Ni-NTA agarose column chromatography
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HisTrap column chromatography and Ni-NTA agarose column chromatography
HisTrap column chromatography and Ni-NTA agarose column chromatography
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expressed in Escherichia coli
expressed in Escherichia coli BL21(DE3)pLysS cells
expressed in Escherichia coli BL21-CodonPlus(DE3)-RIPL cells
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expressed in Escherichia coli BL21(DE3)pLysS cells
expressed in Escherichia coli BL21(DE3)pLysS cells
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C15A/C17A
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the mutant displays a decarboxylation activity similar to that of the wild type enzyme
H169A/D171A
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the mutant is devoid of the ability to perform 2-oxoglutarate turnover
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2-oxoglutarate decarboxylase deficiency
ALKBH4 depletion in mice leads to spermatogenic defects.
2-oxoglutarate decarboxylase deficiency
ALKBH4-dependent demethylation of actin regulates actomyosin dynamics.
Hepatic Encephalopathy
The two catalytic components of the 2-oxoglutarate dehydrogenase complex in rat cerebral synaptic and nonsynaptic mitochondria: comparison of the response to in vitro treatment with ammonia, hyperammonemia, and hepatic encephalopathy.
Liver Failure
The two catalytic components of the 2-oxoglutarate dehydrogenase complex in rat cerebral synaptic and nonsynaptic mitochondria: comparison of the response to in vitro treatment with ammonia, hyperammonemia, and hepatic encephalopathy.
Tuberculosis
Activity-based metabolomic profiling of enzymatic function: identification of Rv1248c as a mycobacterial 2-hydroxy-3-oxoadipate synthase.
Tuberculosis
Variant tricarboxylic acid cycle in Mycobacterium tuberculosis: identification of alpha-ketoglutarate decarboxylase.
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Faff-Michalak, L.; Albrecht, J.
The two catalytic components of the 2-oxoglutarate dehydrogenase complex in rat cerebral synaptic and nonsynaptic mitochondria: Comparison of the response to in vitro treatment with ammonia, hyperammonemia, and hepatic encephalopathy
Neurochem. Res.
18
119-123
1993
Rattus norvegicus
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Shigeoka, S.; Onishi, T.; Maeda, K.; Nakano, Y.; Kitaoka, S.
Occurence of thiamin pyrophopshate-dependent 2-oxoglutarate decarboxylase in mitochondria of Euglena gracilis
FEBS Lett.
195
43-47
1986
Euglena gracilis
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Shigeoka, S.; Nakano, Y.
Characterization and molecular properties of 2-oxoglutarate decarboxylase from Euglena gracilis
Arch. Biochem. Biophys.
288
22-28
1991
Euglena gracilis
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Kapol, R.; Radler, F.
Purification and characterization of 2-oxoglutarate decarboxylase of Leuconostoc mesenteroides
J. Gen. Microbiol.
136
1497-1499
1990
Oenococcus oeni, Oenococcus oeni B 211
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Shigeoka, S.; Hanaoka, T.; Kishi, N.; Nakano, Y.
Effect of L-glutamate on 2-oxoglutarate decarboxylase in Euglena gracilis
Biochem. J.
282
319-323
1992
Euglena gracilis, Euglena gracilis SM-ZK
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Shigeoka, S.; Nakano, Y.
The effect of thiamin on the activation of thiamin pyrophosphate-dependent 2-oxoglutarate decarboxylase in Euglena gracilis
Biochem. J.
292
463-467
1993
Euglena gracilis
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Tian, J.; Bryk, R.; Itoh, M.; Suematsu, M.; Nathan, C.
Variant tricarboxylic acid cycle in Mycobacterium tuberculosis: identification of alpha-ketoglutarate decarboxylase
Proc. Natl. Acad. Sci. USA
102
10670-10675
2005
Mycobacterium tuberculosis
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Bjornstad, L.G.; Zoppellaro, G.; Tomter, A.B.; Falnes, P.O.; Andersson, K.K.
Spectroscopic and magnetic studies of wild-type and mutant forms of the Fe(II)- and 2-oxoglutarate-dependent decarboxylase ALKBH4
Biochem. J.
434
391-398
2011
Homo sapiens
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Wagner, T.; Barilone, N.; Alzari, P.M.; Bellinzoni, M.
A dual conformation of the post-decarboxylation intermediate is associated with distinct enzyme states in mycobacterial KGD (alpha-ketoglutarate decarboxylase)
Biochem. J.
457
425-434
2014
Mycobacterium smegmatis (A0R3B1)
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Wagner, T.; Bellinzoni, M.; Wehenkel, A.; OHare, H.M.; Alzari, P.M.
Functional plasticity and allosteric regulation of alpha-ketoglutarate decarboxylase in central mycobacterial metabolism
Chem. Biol.
18
1011-1020
2011
Mycobacterium smegmatis (A0R2B1), Mycobacterium smegmatis mc(2)155 / ATCC 700084 (A0R2B1), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
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