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EC Tree
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
alkbh4, 2-oxoglutarate decarboxylase, alpha-ketoglutarate decarboxylase, fe(ii)/2og-dependent decarboxylase,
more
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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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alpha-ketoglutarate decarboxylase
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Kgd
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2-oxoglutarate = succinate semialdehyde + CO2
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2-oxoglutarate carboxy-lyase (succinate-semialdehyde-forming)
Requires thiamine diphosphate. Highly specific.
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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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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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?
additional information
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no substrates: pyruvic acid, benzoylformic acid, 2-oxopentanoic acid, 4-methyl-2-oxopentanoic acid and 3-methyl-2-oxobutanoic acid. Enzyme additionally displays low acetolactate synthase activity
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additional information
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the enzyme has pretty low activity of acetolactate synthase. The enzyme does not catalyze the decarboxylation of any of pyruvic acid, benzoylformic acid, 2-oxopentanoic acid, 4-methyl-2-oxopentanoic acid and 3-methyl-2-oxobutanoic acid to form corresponding aldehyde
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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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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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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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thiamine diphosphate
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required
thiamine diphosphate
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required
thiamine diphosphate
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required for activity
thiamine diphosphate
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Km: 0.056 mM
thiamine diphosphate
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0.03 mM
thiamine diphosphate
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Km-value 0.019 mM
thiamine diphosphate
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Km value 0.031 mM
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Ca2+
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no effect
Ca2+
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can partially replace Mg2+ in activation
Ca2+
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2 mM, 1.8fold increase in activity
Ca2+
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about 1.8fold increase of activity at 2 mM
Co2+
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no effect
Co2+
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can partially replace Mg2+ in activation
Mg2+
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strictly required, Km-value 0.196 mM
Mg2+
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2 mM, 2.3fold increase in activity. Km value 0.059 mM
Mg2+
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best stimulant, about 2.3fold increase of activity at 2 mM (used in assay conditions)
MgCl2
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required
Mn2+
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stimulates
Mn2+
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2 mM, 2.2fold increase in activity
Mn2+
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about 2.2fold increase of activity at 2 mM
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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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Co2+
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Co2+
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2 mM, 70% residual activity; about 60% residual activity at 2 mM Co2+
Cu2+
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Cu2+
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2 mM, 70% residual activity; about 50% residual activity at 2 mM Co2+
Hg2+
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Zn2+
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Zn2+
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2 mM, no residual activity; the activity of the enzyme vanishes at 2 mM 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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2-oxoglutarate decarboxylase deficiency
ALKBH4 depletion in mice leads to spermatogenic defects.
2-oxoglutarate decarboxylase deficiency
ALKBH4-dependent demethylation of actin regulates actomyosin dynamics.
Carcinogenesis
ALKBH4 promotes tumourigenesis with a poor prognosis in non-small-cell lung cancer.
Colorectal Neoplasms
ALKBH4 Functions as a Suppressor of Colorectal Cancer Metastasis via Competitively Binding to WDR5.
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.
Lung Neoplasms
ALKBH4 promotes tumourigenesis with a poor prognosis in non-small-cell lung cancer.
Neoplasm Metastasis
ALKBH4 Functions as a Suppressor of Colorectal Cancer Metastasis via Competitively Binding to WDR5.
Neoplasms
ALKBH4 Functions as a Suppressor of Colorectal Cancer Metastasis via Competitively Binding to WDR5.
Neoplasms
ALKBH4 promotes tumourigenesis with a poor prognosis in non-small-cell lung cancer.
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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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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0.19
2-oxoglutarate
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pH 7.0, 25°C
0.19
2-oxoglutarate
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at pH 7.0 and 25°C
0.33
2-oxoglutarate
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pH 7.0
0.33
2-oxoglutarate
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pH 7.0, 30°C
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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1.2
2-oxoglutarate
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pH 7.0, 25°C
1.2
2-oxoglutarate
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at pH 7.0 and 25°C
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6.3
2-oxoglutarate
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pH 7.0, 25°C
6.3
2-oxoglutarate
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at pH 7.0 and 25°C
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4 - 6.5
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active in the range
6
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34% residual activity
6 - 9
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pH 6.0: 65% of activity maximum, pH 9.0: 55% of activity maximum
6.5 - 7
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the optimal pH for the enzyme is at the range of 6.5-7.0. The activity of the enzyme is 34% and 17% at pH 6.0 and 8.0, respectively
8
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17% residual activity
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35 - 40
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35-40°C: activity maximum, maximum activity is maintained up to 60°C
40
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less than 50% of maximum activity below
40 - 55
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the enzyme activity drops by 50% at temperature lower than 40°C, is 70% at 55°C and almost lost at 60°C
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4.2
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isoelectric focusing
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brenda
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brenda
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brenda
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brenda
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UniProt
brenda
B 211
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brenda
B 211
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brenda
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brenda
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brenda
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brenda
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brenda
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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brenda
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UniProt
brenda
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UniProt
brenda
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brenda
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N-terminal 18 amino acids of alpha-KDE1 contain overlapping mitochondrion- and peroxisome-targeting sequences and are sufficient to direct localization to the glycosome
brenda
additional information
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not: cytosol, microsomes
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brenda
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exclusively
brenda
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synaptic and nonsynaptic
brenda
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physiological function
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Despite the lack of a functional Krebs cycle, x02alpha-KDE1 is expressed in bloodstream form of Trypanosoma brucei. RNAi treatment of alpha-KDE1 mRNA results in rapid growth arrest and killing. Cell death is preceded by progressive swelling of the flagellar pocket as a consequence of recruitment of both flagellar and plasma membranes into the pocket
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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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homotetramer
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4 * 60000, SDS-PAGE
homodimer
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x-ray crystallography
homodimer
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x-ray crystallography
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homodimer
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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tetramer
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4 * 62000, SDS-PAGE
tetramer
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4 * 60000, SDS-PAGE, * 61667, calcuated from sequence, recombinant protein with His-tag
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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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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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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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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
67
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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
Ni-NTA resin column chromatography, and Superdex 200 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
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expressed in Escherichia coli
expressed in Escherichia coli BL21(DE3) cells
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expressed in Escherichia coli BL21(DE3)pLysS cells
expressed in Escherichia coli BL21-CodonPlus(DE3)-RIPL cells
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expression in Escherichia coli
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expression in Trypanosoma brucei
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expressed in Escherichia coli BL21(DE3)pLysS cells
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expressed in Escherichia coli BL21(DE3)pLysS cells
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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
brenda
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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brenda
Shigeoka, S.; Nakano, Y.
Characterization and molecular properties of 2-oxoglutarate decarboxylase from Euglena gracilis
Arch. Biochem. Biophys.
288
22-28
1991
Euglena gracilis
brenda
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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brenda
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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brenda
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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brenda
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
brenda
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
brenda
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
Mycolicibacterium smegmatis (A0R3B1)
brenda
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 tuberculosis, Mycolicibacterium smegmatis (A0R2B1), Mycolicibacterium smegmatis mc(2)155 / ATCC 700084 (A0R2B1), Mycobacterium tuberculosis H37Rv
brenda
Sykes, S.; Szempruch, A.; Hajduk, S.
The Krebs cycle enzyme alpha-ketoglutarate decarboxylase is an essential glycosomal protein in bloodstream African trypanosomes
Eukaryot. Cell
14
206-215
2015
Trypanosoma brucei
brenda
Lei, G.; Wang, X.; Lai, C.; Li, Z.M.; Zhang, W.; Xie, C.; Wang, F.; Wu, X.; Li, Z.
Expression and biochemical characterization of alpha-ketoglutarate decarboxylase from cyanobacterium Synechococcus sp. PCC7002
Int. J. Biol. Macromol.
114
188-193
2018
Synechococcus sp. PCC 7002
brenda
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