HOME
login
history
all enzymes
BRENDA home
History
Information on EC 4.1.1.71 - 2-oxoglutarate decarboxylase
for references in articles please use BRENDA:EC4.1.1.71Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
4.1.1.71 2-oxoglutarate decarboxylaseIUBMB Comments
Requires thiamine diphosphate. Highly specific.
Specify your search results
Word Map
- 4.1.1.71
- thiamin
-
tricarboxylic
-
multienzyme
- lipoamide
-
lipoic
- euglena
-
pigeon
-
lipoyl-lysine
- tpp
- menaquinone
- shchc
- isochorismate
- succinyltransferase
-
mend
The enzyme appears in viruses and cellular organisms
Synonyms
ALKBH4, alpha-ketoglutarate decarboxylase, alpha-ketoglutaric decarboxylase, alpha-KGD, decarboxylase, oxoglutarate, E1o, Fe(II)/2OG-dependent decarboxylase, KDC, Kgd, oxoglutarate decarboxylase, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
alpha-ketoglutarate decarboxylase
alpha-ketoglutaric decarboxylase
-
-
-
-
decarboxylase, oxoglutarate
-
-
-
-
KDC
-
-
-
-
Kgd
oxoglutarate decarboxylase
-
-
-
-
pre-2-oxoglutarate decarboxylase
-
-
-
-
alpha-ketoglutarate decarboxylase
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2-oxoglutarate = succinate semialdehyde + CO2
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
decarboxylation
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
2-oxoglutarate carboxy-lyase (succinate-semialdehyde-forming)
Requires thiamine diphosphate. Highly specific.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
37205-42-8
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-oxoglutarate
succinate semialdehyde + CO2
Mycolicibacterium smegmatis mc(2)155 / ATCC 700084
-
-
-
?
additional information
?
-
-
the enzyme has a physiologically important role coupling with succinate-semialdehyde dehydrogenase in the tricarboxylic acid cycle
-
-
-
additional information
?
-
-
enzyme has physiological function in the assimilation of L-glutamate
-
-
-
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
?
-
-
the 2-oxoglutarate dehydrogenase complex: 2-oxoglutarate decarboxylase and lipoamide dehydrogenase is a rate-limiting mitochondrial enzyme of the tricarboxylic acid cycle
-
-
-
additional information
?
-
-
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
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-oxoglutarate
succinate semialdehyde + CO2
Mycolicibacterium smegmatis mc(2)155 / ATCC 700084
-
-
-
?
additional information
?
-
-
the enzyme has a physiologically important role coupling with succinate-semialdehyde dehydrogenase in the tricarboxylic acid cycle
-
-
-
additional information
?
-
-
enzyme has physiological function in the assimilation of L-glutamate
-
-
-
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
?
-
-
the 2-oxoglutarate dehydrogenase complex: 2-oxoglutarate decarboxylase and lipoamide dehydrogenase is a rate-limiting mitochondrial enzyme of the tricarboxylic acid cycle
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Co2+
Mg2+
MgCl2
Mn2+
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NH4Cl
-
preferential sensitivity of enzyme to NH4Cl in vitro in nonsynaptic mitochondria and hyperammonemic conditions in vivo in synaptic mitochondria
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
comparison of the effect of NH4Cl in vitro, hepatic encephalopathy, and hyperammonemia on KM in synaptic and nonsynaptic brain mitochondria
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
35 - 40
-
35-40°C: activity maximum, maximum activity is maintained up to 60°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
lacking a 2-oxoglutarate dehydrogenase complex (EC 1.2.4.2 + EC 2.3.1.61 + EC 1.8.1.4)
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
-
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
Show AA Sequence and Transmembrane Helices (1913 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PDB
SCOP
CATH
UNIPROT
ORGANISM
Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155)
Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155)
Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155)
Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155)
Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155)
Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155)
Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155)
Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155)
Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155)
Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155)
Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155)
Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155)
Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155)
Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155)
Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155)
Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155)
Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155)
Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155)
Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155)
Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homodimer
monomer
tetramer
homodimer
Mycolicibacterium smegmatis mc(2)155 / ATCC 700084
-
x-ray crystallography
-
tetramer
-
4 * 60000, SDS-PAGE, * 61667, calcuated from sequence, recombinant protein with His-tag
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PROTEIN VARIANTS
ORGANISM
UNIPROT
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
70
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
HisTrap column chromatography and Ni-NTA agarose column chromatography
HisTrap column chromatography and Ni-NTA agarose column chromatography
-
HisTrap column chromatography and Ni-NTA agarose column chromatography
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3)pLysS cells
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
-
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
-
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
-
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
-
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, Mycobacterium tuberculosis H37Rv, Mycolicibacterium smegmatis (A0R2B1), Mycolicibacterium smegmatis mc(2)155 / ATCC 700084 (A0R2B1)
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
Select items on the left to see more content.
EXTERNAL LINKS (specific for EC-Number 4.1.1.71)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Information
