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 hide
4.1.1.71
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RECOMMENDED NAME
GeneOntology No.
2-oxoglutarate decarboxylase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2-oxoglutarate = succinate semialdehyde + CO2
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
decarboxylation
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
TCA cycle IV (2-oxoglutarate decarboxylase)
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SYSTEMATIC NAME
IUBMB Comments
2-oxoglutarate carboxy-lyase (succinate-semialdehyde-forming)
Requires thiamine diphosphate. Highly specific.
CAS REGISTRY NUMBER
COMMENTARY hide
37205-42-8
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain SM-ZK
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
B 211
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Manually annotated by BRENDA team
B 211
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-oxoglutarate
succinate semialdehyde + CO2
show the reaction diagram
oxaloacetate
?
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
2-oxoglutarate
succinate semialdehyde + CO2
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ATP
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slight stimulation
NADP+
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stimulates
NADPH
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stimulates
thiamine diphosphate
additional information
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no cofactor: coenzyme A, NAD+, NADP+
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe2+
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dependent on
Mg2+
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strictly required, Km-value 0.196 mM
Mn2+
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stimulates
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
2,4-Dinitrophenol
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2-oxoglutarate
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above 2 mM substrate inhibition
isocitrate
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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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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
2-oxoglutarate
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citrate
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DL-malate
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fumarate
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L-alanine
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L-aspartate
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L-glutamate
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activation is abolished by the simultaneous addition of cycloheximide
L-lactate
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Propionate
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pyruvate
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succinate
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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
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.33 - 1
2-oxoglutarate
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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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35 - 40
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35-40C: activity maximum, maximum activity is maintained up to 60C
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.2
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isoelectric focusing
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
additional information
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not: cytosol, microsomes
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Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
70000
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PAGE
250000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
homodimer
monomer
tetramer
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4 * 62000, SDS-PAGE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.2 - 8.5
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62C, 10 min, stable
648365
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
GENERAL STABILITY
ORGANISM
UNIPROT
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
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4C or -20C, 24 h, 95% or 25% loss of activity, respectively
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
glutathione-Sepharose column chromatography, gel filtration
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HisTrap column chromatography and Ni-NTA agarose column chromatography
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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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