Information on EC 4.1.1.71 - 2-oxoglutarate decarboxylase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY
4.1.1.71
-
RECOMMENDED NAME
GeneOntology No.
2-oxoglutarate decarboxylase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
2-oxoglutarate = succinate semialdehyde + CO2
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
decarboxylation
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
TCA cycle IV (2-oxoglutarate decarboxylase)
-
SYSTEMATIC NAME
IUBMB Comments
2-oxoglutarate carboxy-lyase (succinate-semialdehyde-forming)
Requires thiamine diphosphate. Highly specific.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
ALKBH4
-
-
alpha-ketoglutarate decarboxylase
-
-
-
-
alpha-ketoglutaric decarboxylase
-
-
-
-
decarboxylase, oxoglutarate
-
-
-
-
Fe(II)/2OG-dependent decarboxylase
-
-
KDC
-
-
-
-
oxoglutarate decarboxylase
-
-
-
-
pre-2-oxoglutarate decarboxylase
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
37205-42-8
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
lacking a 2-oxoglutarate dehydrogenase complex (EC 1.2.4.2 + EC 2.3.1.61 + EC 1.8.1.4)
-
-
Manually annotated by BRENDA team
strain SM-ZK
-
-
Manually annotated by BRENDA team
Euglena gracilis SM-ZK
strain SM-ZK
-
-
Manually annotated by BRENDA team
Oenococcus oeni B 211
B 211
-
-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-oxoglutarate
succinate semialdehyde + CO2
show the reaction diagram
-
-
-
-
?
2-oxoglutarate
succinate semialdehyde + CO2
show the reaction diagram
-
-
-
?
2-oxoglutarate
succinate semialdehyde + CO2
show the reaction diagram
-
-
-
?
2-oxoglutarate
succinate semialdehyde + CO2
show the reaction diagram
-
-
-
-
?
2-oxoglutarate
succinate semialdehyde + CO2
show the reaction diagram
-
-
-
-
?
2-oxoglutarate
succinate semialdehyde + CO2
show the reaction diagram
-
highly specific
-
?
2-oxoglutarate
succinate semialdehyde + CO2
show the reaction diagram
-
highly specific
-
-
?
2-oxoglutarate
succinate semialdehyde + CO2
show the reaction diagram
Oenococcus oeni B 211
-
-
-
-
?
oxaloacetate
?
show the reaction diagram
Oenococcus oeni, Oenococcus oeni B 211
-
28% of the activity with 2-oxoglutarate
-
-
?
2-oxoglutarate
succinate semialdehyde + CO2
show the reaction diagram
Euglena gracilis SM-ZK
-
-
-
?
additional information
?
-
-
the enzyme has a physiologically important role coupling with succinate-semialdehyde dehydrogenase in the tricarboxylic acid cycle
-
-
-
additional information
?
-
-
the 2-oxoglutarate dehydrogenase complex: 2-oxoglutarate decarboxylase and lipoamide dehydrogenase is a rate-limiting mitochondrial enzyme of the tricarboxylic acid cycle
-
-
-
additional information
?
-
-
enzyme has physiological function in the assimilation of L-glutamate
-
-
-
additional information
?
-
-
enzyme and GabD1 or GabD2 form an alternative pathway from 2-oxoglutarate to succinate, no substrate: pyruvate
-
-
-
additional information
?
-
Euglena gracilis SM-ZK
-
enzyme has physiological function in the assimilation of L-glutamate
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
the enzyme has a physiologically important role coupling with succinate-semialdehyde dehydrogenase in the tricarboxylic acid cycle
-
-
-
additional information
?
-
-
the 2-oxoglutarate dehydrogenase complex: 2-oxoglutarate decarboxylase and lipoamide dehydrogenase is a rate-limiting mitochondrial enzyme of the tricarboxylic acid cycle
-
-
-
additional information
?
-
-
enzyme has physiological function in the assimilation of L-glutamate
-
-
-
additional information
?
-
-
enzyme and GabD1 or GabD2 form an alternative pathway from 2-oxoglutarate to succinate
-
-
-
additional information
?
-
Euglena gracilis SM-ZK
-
enzyme has physiological function in the assimilation of L-glutamate
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
NADPH
-
stimulates
thiamine diphosphate
-
Km: 0.056 mM; required
thiamine diphosphate
-
0.03 mM; required
thiamine diphosphate
-
Km-value 0.019 mM
ATP
-
slight stimulation
additional information
-
no cofactor: coenzyme A, NAD+, NADP+
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ca2+
-
can partially replace Mg2+ in activation
Ca2+
-
no effect
Co2+
-
can partially replace Mg2+ in activation
Co2+
-
no effect
Fe2+
-
dependent on
Mg2+
-
strictly required, Km-value 0.196 mM
MgCl2
-
required
MgCl2
-
Km: 0.093 mM; stimulates
Mn2+
-
stimulates
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1,10-phenanthroline
-
-
1,10-phenanthroline
-
-
2,4-Dinitrophenol
-
-
2-oxoglutarate
-
above 2 mM substrate inhibition
Fe2+
-
-
-
NH4Cl
-
preferential sensitivity of enzyme to NH4Cl in vitro in nonsynaptic mitochondria and hyperammonemic conditions in vivo in synaptic mitochondria
Succinic semialdehyde
-
-
m-chlorophenylhydrazone
-
-
additional information
-
not: NaN3
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2-mercaptoethanol
-
stimulates
2-mercaptoethanol
-
stimulates
2-oxoglutarate
-
-
DTT
-
stimulates
L-aspartate
-
-
L-glutamate
-
activation is abolished by the simultaneous addition of cycloheximide
thiamine
-
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
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.33
-
2-oxoglutarate
-
pH 7.0, 30C
0.33
-
2-oxoglutarate
-
pH 7.0
0.48
-
2-oxoglutarate
-
22C, pH 7.0
1
-
2-oxoglutarate
-
pH 5.3, 30C
additional information
-
additional information
-
comparison of the effect of NH4Cl in vitro, hepatic encephalopathy, and hyperammonemia on KM in synaptic and nonsynaptic brain mitochondria
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4
6.5
-
active in the range
6
9
-
pH 6.0: 65% of activity maximum, pH 9.0: 55% of activity maximum
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
35
40
-
35-40C: activity maximum, maximum activity is maintained up to 60C
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4.2
-
-
isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
synaptic and nonsynaptic
Manually annotated by BRENDA team
additional information
-
not: cytosol, microsomes
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
70000
-
-
PAGE
250000
-
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
monomer
-
1 * 65000, SDS-PAGE
monomer
Oenococcus oeni B 211
-
1 * 65000, SDS-PAGE
-
tetramer
-
4 * 62000, SDS-PAGE
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.2
8.5
-
62C, 10 min, stable
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
57.5
-
-
10 min, stable up to
60
-
-
pH 5.3, 30 min, 10% loss of activity
62
-
-
pH 6.2-8.5, 10 min, stable
67
-
-
10 min, complete loss of activity
70
-
-
complete loss of activity at 70C
70
-
-
pH 5.3, 5 min, 90% loss of activity
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
the isolated proteins (ALKBH4 and mutants), even when kept in iced-cooled solutions (4C), 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
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
4C or -20C, 24 h, 95% or 25% loss of activity, respectively
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
glutathione-Sepharose column chromatography, gel filtration
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expressed in Escherichia coli BL21-CodonPlus(DE3)-RIPL cells
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
C15A/C17A
-
the mutant displays a decarboxylation activity similar to that of the wild type enzyme
H169A/D171A
-
the mutant is devoid of the ability to perform 2-oxoglutarate turnover