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Information on EC 2.2.1.5 - 2-hydroxy-3-oxoadipate synthase
for references in articles please use BRENDA:EC2.2.1.5
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EC Tree 2 Transferases
2.2 Transferring aldehyde or ketonic groups
2.2.1 Transketolases and transaldolases
2.2.1.5 2-hydroxy-3-oxoadipate synthase
IUBMB Comments
The bacterial enzyme requires thiamine diphosphate. The product decarboxylates to 5-hydroxy-4-oxopentanoate. The enzyme can decarboxylate 2-oxoglutarate. Acetaldehyde can replace glyoxylate.
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
- 2.2.1.5
- thiamin
- acetaldehyde
- benzaldehyde
-
diphosphate-dependent
-
carboligation
-
thdp-dependent
-
zymomonas
-
r-phenylacetylcarbinol
- mobilis
- benzoylformate
- hyperoxaluria
- utilis
-
r-benzoin
-
enamine
-
1',4'-iminopyrimidine
-
thdp-bound
-
thiamine-deficient
- medicine
- synthesis
showSynonyms
carboligase, rv1248c, 2-hydroxy-3-oxoadipate synthase, alpha-ketoglutarate:glyoxylate carboligase, hoa synthase, 2-oxoglutarate glyoxylate carboligase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
(R)-HOA synthase
2-hydroxy-3-oxoadipate glyoxylate-lyase (carboxylating)
-
-
-
-
2-hydroxy-3-oxoadipate synthase
2-oxoglutarate: glyoxylate carboligase
-
-
-
-
alpha-ketoglutarate:glyoxylate carboligase
-
-
-
-
alpha-ketoglutaric-glyoxylic carboligase
-
-
-
-
carboligase
EC 4.1.3.15
-
-
formerly
-
glyoxylate-2-oxoglutarate carboligase
-
-
-
-
HOA synthase
HOAS
Kgd
oxoglutarate: glyoxylate carboligase
-
-
-
-
Rv1248c
carboligase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
2-oxoglutarate + glyoxylate = 2-hydroxy-3-oxoadipate + CO2
various alternative mechanisms proposed
-
2-oxoglutarate + glyoxylate = 2-hydroxy-3-oxoadipate + CO2
mechanism
-
2-oxoglutarate + glyoxylate = 2-hydroxy-3-oxoadipate + CO2
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
decarboxylation
-
-
synergistic
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
2-oxoglutarate:glyoxylate succinaldehydetransferase (decarboxylating)
The bacterial enzyme requires thiamine diphosphate. The product decarboxylates to 5-hydroxy-4-oxopentanoate. The enzyme can decarboxylate 2-oxoglutarate. Acetaldehyde can replace glyoxylate.
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CAS REGISTRY NUMBER
COMMENTARY
9054-72-2
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-oxoglutarate + ethyl glyoxylate
(R)-6-ethoxy-5-hydroxy-4,6-dioxohexanoic acid + CO2
Substrates: -
Products: 81% enantiomeric excess
Products: 81% enantiomeric excess
?
2-oxoglutarate + glyoxylate
(R)-2-hydroxy-3-oxoadipate + CO2
Substrates: -
Products: 90% enantiomeric excess
Products: 90% enantiomeric excess
?
2-oxoglutarate + methylglyoxal
(R)-5-hydroxy-4,6-dioxoheptanoic acid + CO2
Substrates: -
Products: 83% enantiomeric excess
Products: 83% enantiomeric excess
?
2-oxoisovalerate + ethyl glyoxylate
(S)-ethyl 2-hydroxy-4-methyl-3-oxopentanoic acid + CO2
Substrates: -
Products: 81% enantiomeric excess
Products: 81% enantiomeric excess
?
2-oxoisovalerate + glyoxylate
(S)-2-hydroxy-4-methyl-3-oxopentanoic acid + CO2
Substrates: -
Products: 67% enantiomeric excess
Products: 67% enantiomeric excess
?
2-oxoisovalerate + methylglyoxal
(S)-3-hydroxy-5-methylhexane-2,4-dione + CO2
Substrates: -
Products: more than 90% enantiomeric excess
Products: more than 90% enantiomeric excess
?
2-oxovalerate + ethyl glyoxylate
(S)-ethyl 2-hydroxy-3-oxohexanoic acid + CO2
Substrates: -
Products: 52% enantiomeric excess
Products: 52% enantiomeric excess
?
2-oxovalerate + glyoxylate
(S)-2-hydroxy-3-oxohexanoic acid + CO2
Substrates: -
Products: 96% enantiomeric excess
Products: 96% enantiomeric excess
?
2-oxovalerate + methylglyoxal
(S)-3-hydroxyheptane-2,4-dione + CO2
Substrates: -
Products: 81% enantiomeric excess
Products: 81% enantiomeric excess
?
2-oxoglutarate
? + CO2
-
Substrates: identical with 2-oxoglutarate decarboxylase
Products: -
Products: -
?
2-oxoglutarate + acetaldehyde
5-hydroxy-4-oxohexanoate + CO2
-
Substrates: -
Products: -
Products: -
?
2-oxoglutarate + acetaldehyde
5-hydroxy-4-oxohexanoate + CO2
-
Substrates: -
Products: -
Products: -
?
2-oxoglutarate + acetaldehyde
5-hydroxy-4-oxohexanoate + CO2
-
Substrates: -
Products: -
Products: -
?
2-oxoglutarate + glyoxylate
2-hydroxy-3-oxoadipate + CO2
-
Substrates: -
Products: -
Products: -
?
2-oxoglutarate + glyoxylate
2-hydroxy-3-oxoadipate + CO2
Substrates: -
Products: -
Products: -
?
2-oxoglutarate + glyoxylate
2-hydroxy-3-oxoadipate + CO2
-
Substrates: -
Products: -
Products: -
?
2-oxoglutarate + glyoxylate
2-hydroxy-3-oxoadipate + CO2
-
Substrates: -
Products: -
Products: -
?
2-oxoglutarate + glyoxylate
2-hydroxy-3-oxoadipate + CO2
Substrates: -
Products: -
Products: -
?
2-oxoglutarate + glyoxylate
2-hydroxy-3-oxoadipate + CO2
-
Substrates: -
Products: -
Products: -
?
2-oxoglutarate + glyoxylate
2-hydroxy-3-oxohexandioate + CO2
-
Substrates: -
Products: i. e. 2-hydroxy-3-oxoadipic acid
Products: i. e. 2-hydroxy-3-oxoadipic acid
?
2-oxoglutarate + glyoxylate
2-hydroxy-3-oxohexandioate + CO2
-
Substrates: -
Products: also 2,3-dihydroxy-4-ketopimelic acid
Products: also 2,3-dihydroxy-4-ketopimelic acid
?
2-oxoglutarate + glyoxylate
2-hydroxy-3-oxohexandioate + CO2
-
Substrates: -
Products: further decarboxylation leads to 5-hydroxy-4-ketovaleric acid
Products: further decarboxylation leads to 5-hydroxy-4-ketovaleric acid
?
2-oxoglutarate + glyoxylate
2-hydroxy-3-oxohexandioate + CO2
-
Substrates: -
Products: -
Products: -
?
2-oxoglutarate + glyoxylate
2-hydroxy-3-oxohexandioate + CO2
-
Substrates: -
Products: further spontaneous decarboxylation in the presence of acid
Products: further spontaneous decarboxylation in the presence of acid
?
2-oxoglutarate + glyoxylate
2-hydroxy-3-oxohexandioate + CO2
-
Substrates: -
Products: -
Products: -
?
2-oxoglutarate + glyoxylate
2-hydroxy-3-oxohexandioate + CO2
-
Substrates: -
Products: -
Products: -
?
2-oxoglutarate + glyoxylate
2-hydroxy-3-oxohexandioate + CO2
-
Substrates: -
Products: -
Products: -
?
2-oxoglutarate + glyoxylate
2-hydroxy-3-oxohexandioate + CO2
-
Substrates: -
Products: -
Products: -
?
2-oxoglutarate + glyoxylate
2-hydroxy-3-oxohexandioate + CO2
-
Substrates: -
Products: -
Products: -
?
2-oxoglutarate + glyoxylate
2-hydroxy-3-oxohexandioate + CO2
-
Substrates: -
Products: i. e. 2-hydroxy-3-oxoadipic acid
Products: i. e. 2-hydroxy-3-oxoadipic acid
?
2-oxoglutarate + glyoxylate
2-hydroxy-3-oxohexandioate + CO2
-
Substrates: -
Products: further spontaneous decarboxylation in the presence of acid
Products: further spontaneous decarboxylation in the presence of acid
?
2-oxoglutarate + glyoxylate
2-hydroxy-3-oxohexandioate + CO2
-
Substrates: -
Products: -
Products: -
?
2-oxoglutarate + glyoxylate
?
-
Substrates: possible 1-carbon source for nicotine synthesis
Products: -
Products: -
?
2-oxoglutarate + glyoxylate
?
-
Substrates: linked to citric acid cycle
Products: -
Products: -
?
2-oxoglutarate + glyoxylate
?
-
Substrates: linked to citric acid cycle
Products: -
Products: -
?
2-oxoglutarate + glyoxylate
?
-
Substrates: important as diversion of glyoxylate from oxalate formation
Products: -
Products: -
?
2-oxoglutarate + glyoxylate
?
-
Substrates: hypothesized 2-oxoglutarate regeneration cycle
Products: -
Products: -
?
additional information
?
-
Substrates: Rv1248c catalyzes C-C bond formation between the activated aldehyde of alpha-ketoglutarate and the carbonyl of glyoxylate to yield 2-hydroxy-3-oxoadipate (HOA), which decomposes to 5-hydroxylevulinate
Products: -
Products: -
?
additional information
?
-
-
Substrates: Rv1248c catalyzes C-C bond formation between the activated aldehyde of alpha-ketoglutarate and the carbonyl of glyoxylate to yield 2-hydroxy-3-oxoadipate (HOA), which decomposes to 5-hydroxylevulinate
Products: -
Products: -
?
additional information
?
-
Substrates: catalyzing C-C bond formation between the activated aldehyde formed after decarboxylation of alpha-ketoglutarate and the carbonyl of a second substrate, glyoxylate (GLX), to yield 2-hydroxy-3-oxoadipate (HOA)
Products: -
Products: -
?
additional information
?
-
-
Substrates: catalyzing C-C bond formation between the activated aldehyde formed after decarboxylation of alpha-ketoglutarate and the carbonyl of a second substrate, glyoxylate (GLX), to yield 2-hydroxy-3-oxoadipate (HOA)
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme catalyzes consumption of 2-oxoglutarate in a mycobacterial small molecule extract with matched production of 5-hydroxylevulinate (HLA) in a reaction predicted to require glyoxylate
Products: -
Products: -
?
additional information
?
-
-
Substrates: enzyme catalyzes consumption of 2-oxoglutarate in a mycobacterial small molecule extract with matched production of 5-hydroxylevulinate (HLA) in a reaction predicted to require glyoxylate
Products: -
Products: -
?
additional information
?
-
Substrates: Rv1248c catalyzes C-C bond formation between the activated aldehyde of alpha-ketoglutarate and the carbonyl of glyoxylate to yield 2-hydroxy-3-oxoadipate (HOA), which decomposes to 5-hydroxylevulinate
Products: -
Products: -
?
additional information
?
-
Substrates: catalyzing C-C bond formation between the activated aldehyde formed after decarboxylation of alpha-ketoglutarate and the carbonyl of a second substrate, glyoxylate (GLX), to yield 2-hydroxy-3-oxoadipate (HOA)
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme catalyzes consumption of 2-oxoglutarate in a mycobacterial small molecule extract with matched production of 5-hydroxylevulinate (HLA) in a reaction predicted to require glyoxylate
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-oxoglutarate + glyoxylate
2-hydroxy-3-oxoadipate + CO2
-
Substrates: -
Products: -
Products: -
?
2-oxoglutarate + glyoxylate
2-hydroxy-3-oxoadipate + CO2
-
Substrates: -
Products: -
Products: -
?
2-oxoglutarate + glyoxylate
2-hydroxy-3-oxoadipate + CO2
-
Substrates: -
Products: -
Products: -
?
2-oxoglutarate + glyoxylate
?
-
Substrates: possible 1-carbon source for nicotine synthesis
Products: -
Products: -
?
2-oxoglutarate + glyoxylate
?
-
Substrates: linked to citric acid cycle
Products: -
Products: -
?
2-oxoglutarate + glyoxylate
?
-
Substrates: linked to citric acid cycle
Products: -
Products: -
?
2-oxoglutarate + glyoxylate
?
-
Substrates: important as diversion of glyoxylate from oxalate formation
Products: -
Products: -
?
2-oxoglutarate + glyoxylate
?
-
Substrates: hypothesized 2-oxoglutarate regeneration cycle
Products: -
Products: -
?
additional information
?
-
Substrates: Rv1248c catalyzes C-C bond formation between the activated aldehyde of alpha-ketoglutarate and the carbonyl of glyoxylate to yield 2-hydroxy-3-oxoadipate (HOA), which decomposes to 5-hydroxylevulinate
Products: -
Products: -
?
additional information
?
-
-
Substrates: Rv1248c catalyzes C-C bond formation between the activated aldehyde of alpha-ketoglutarate and the carbonyl of glyoxylate to yield 2-hydroxy-3-oxoadipate (HOA), which decomposes to 5-hydroxylevulinate
Products: -
Products: -
?
additional information
?
-
Substrates: catalyzing C-C bond formation between the activated aldehyde formed after decarboxylation of alpha-ketoglutarate and the carbonyl of a second substrate, glyoxylate (GLX), to yield 2-hydroxy-3-oxoadipate (HOA)
Products: -
Products: -
?
additional information
?
-
-
Substrates: catalyzing C-C bond formation between the activated aldehyde formed after decarboxylation of alpha-ketoglutarate and the carbonyl of a second substrate, glyoxylate (GLX), to yield 2-hydroxy-3-oxoadipate (HOA)
Products: -
Products: -
?
additional information
?
-
Substrates: Rv1248c catalyzes C-C bond formation between the activated aldehyde of alpha-ketoglutarate and the carbonyl of glyoxylate to yield 2-hydroxy-3-oxoadipate (HOA), which decomposes to 5-hydroxylevulinate
Products: -
Products: -
?
additional information
?
-
Substrates: catalyzing C-C bond formation between the activated aldehyde formed after decarboxylation of alpha-ketoglutarate and the carbonyl of a second substrate, glyoxylate (GLX), to yield 2-hydroxy-3-oxoadipate (HOA)
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
thiamine diphosphate
-
deficiency may lead to hyperoxaluria and glyoxylate excretion
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mn2+
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
deazathiamine diphosphate
-
binds 32fold more tightly to the enzyme than thiamine diphosphate
GarA
protein GarA involved in phosphorylation-dependent signaling pathway, acts as a dynamic allosteric inhibitor of KGD by preventing crucial motions in KGD that are necessary for catalysis. The GarA binding pocket targets an allosteric site on nonphosphorylated KGD, where a key element of recognition is a phosphomimetic aspartate
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Carcinoma, Hepatocellular
Inhibitory effect of 2'-fluoro-5-methyl-beta-L-arabinofuranosyl-uracil on duck hepatitis B virus replication.
Genetic Diseases, Inborn
Cellular localization of alpha-ketoglutarate: glyoxylate carboligase in rat tissues.
Hepatitis B
Inhibitory effect of 2'-fluoro-5-methyl-beta-L-arabinofuranosyl-uracil on duck hepatitis B virus replication.
Hyperoxaluria
Cellular localization of alpha-ketoglutarate: glyoxylate carboligase in rat tissues.
Hyperoxaluria, Primary
Alanine glyoxylate aminotransferase deficiency: biochemical and molecular genetic lessons from the study of a human disease.
Hyperoxaluria, Primary
Mitochondrial damage and the subcellular distribution of 2-oxoglutarate:glyoxylate carboligase in normal human and rat liver and in the liver of a patient with primary hyperoxaluria type I.
Tuberculosis
Activity-based metabolomic profiling of enzymatic function: identification of Rv1248c as a mycobacterial 2-hydroxy-3-oxoadipate synthase.
Tuberculosis
Comparison of transposon and deletion mutants in Mycobacterium tuberculosis: The case of rv1248c, encoding 2-hydroxy-3-oxoadipate synthase.
Tuberculosis
Functional Plasticity and Allosteric Regulation of ?-Ketoglutarate Decarboxylase in Central Mycobacterial Metabolism.
Tuberculosis
Influence of allosteric regulators on individual steps in the reaction catalyzed by Mycobacterium tuberculosis 2-hydroxy-3-oxoadipate synthase.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.144
deazathiamine
Mycobacterium tuberculosis
-
pH not specified in the publication, temperature not specified in the publication
0.0067
deazathiamine diphosphate
Mycobacterium tuberculosis
-
pH not specified in the publication, temperature not specified in the publication
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
37
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
protein is originally annotated as the alpha-ketoglutarate (alpha-KG) decarboxylase (E1) component of alpha-KG dehydrogenase complex. The physiological activity of Rv1248c as that of a carboligase established by activity-based metabolomic profiling
UniProt
brenda
protein is originally annotated as the alpha-ketoglutarate (alpha-KG) decarboxylase (E1) component of alpha-KG dehydrogenase complex. The physiological activity of Rv1248c as that of a carboligase established by activity-based metabolomic profiling
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
part of alpha-ketoglutarate dehydrogenase complex
brenda
-
part of alpha-ketoglutarate dehydrogenase complex
brenda
-
part of alpha-ketoglutarate dehydrogenase complex
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
malfunction
-
enzyme deletion severely attenuates Mycobacterium tuberculosis in vivo
malfunction
-
enzyme deletion severely attenuates Mycobacterium tuberculosis in vivo
-
malfunction
-
enzyme deletion severely attenuates Mycobacterium tuberculosis in vivo
-
metabolism
GarA involved in phosphorylation-dependent signaling pathway, acts as a dynamic allosteric inhibitor of KGD by preventing crucial motions in KGD that are necessary for catalysis. The GarA binding pocket targets an allosteric site on nonphosphorylated KGD, where a key element of recognition is a phosphomimetic aspartate. Mutations R62A, K141E and R143E in GarA abolish binding
metabolism
-
GarA involved in phosphorylation-dependent signaling pathway, acts as a dynamic allosteric inhibitor of KGD by preventing crucial motions in KGD that are necessary for catalysis. The GarA binding pocket targets an allosteric site on nonphosphorylated KGD, where a key element of recognition is a phosphomimetic aspartate. Mutations R62A, K141E and R143E in GarA abolish binding
-
Show AA Sequence and Transmembrane Helices (828 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.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
structures of the mycobacterial upstream (phosphorylation-dependent) complex PknB-GarA and the downstream (phosphorylation-independent) complex GarA-KGD. The phosphorylated activation loop of PknB serves as a docking site to recruit GarA through canonical FHA-pThr interactions. GarA acts as a dynamic allosteric inhibitor of KGD by preventing crucial motions in KGD that are necessary for catalysis
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, potassium phosphate buffer, pH 7.1, 10% glycerol, 1 mM dithiothreitol, at least several days
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, Q Sepharose column chromatography, Mono Q column chromatography, and Sephacryl S-100 gel filtration
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
synthesis
application of the E1 component of the Escherichia coli 2-oxoglutarate dehydrogenase multienzyme complex in the synthesis of chiral ompounds with multiple functional groups in good yield and high enantiomeric excess, by varying both the donor substrate (different 2-oxo acids) and the acceptor substrate (glyoxylate, ethyl glyoxylate and methyl glyoxal). The enzyme can accept 2-oxovalerate and 2-oxoisovalerate in addition to its natural substrate 2-oxoglutarate, and the tested acceptors are also acceptable in the carboligation reaction
medicine
-
deficiency leads to hyperoxaluria, relative decrease in liver biomass
medicine
-
involved in renal stone formation, decreased activity due to thiamine deficiency may increase oxalate excretion by 35%
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hirabayashi, T.; Harada, T.
Inhibition of the alpha-ketoglutarate dehydrogenase complex from baker's yeast by acetaldehyde and glyoxylate
Agric. Biol. Chem.
36
1249-1251
1972
Saccharomyces cerevisiae
-
brenda
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Cellular localization of alpha-ketoglutarate: glyoxylate carboligase in rat tissues
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Rattus norvegicus, Oryctolagus cuniculus
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Zaror-Behrens, G.; Mavrides, C.
Further studies on 2-oxoglutarate:glyoxylate carboligase activity in Tetrahymena pyriformis
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Tetrahymena pyriformis
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Yamasaki, H.; Moriyama, T.
Purification, general properties and two other catalytic activities of alpha-ketoglutarate:glyoxylate carboligase of Mycobacterium phlei
Biochim. Biophys. Acta
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Mycolicibacterium phlei
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Schlossberg, M.A.; Bloom, R.J.; Richert, D.A.; Westerfeld, W.W.
Carboligase activity of alpha-ketoglutarate dehydrogenase
Biochemistry
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1970
Rattus norvegicus, Bos taurus
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Schlossberg, M.A.; Richert, D.A.; Bloom, R.J.; Westerfeld, W.W.
Isolation and identification of 5-hydroxy-4-ketovaleric acid as a product of alpha-ketoglutarate:glyoxylate carboligase
Biochemistry
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Steward, P.R.; Quale, J.R.
The synergistic decarboxylation of glyoxylate and 2-oxoglutarate by an enzyme system from pig-liver mitochondria
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Rattus norvegicus
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Yamasaki, H.; Mariyama, T.
alpha-Ketoglutarate:glyoxylate carboligase activity in Escherichia coli
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Escherichia coli
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Sidhu, H.; Gupta, R.; Thind, S.K.; Nath, R.
Oxalate metabolism in thiamine-deficient rats
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Prather, C.W.; Sisler, E.C.
Glycine and glyoxylate decarboxylation in Nicotiana rustica roots
Phytochemistry
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Nicotiana rustica
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Bats, R.; Rofe, A.M.; Conyers, R.A.J.
Investigations into the effect of glyoxylate decarboxylation and transamination on oxalate formation in rat
Nephron
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Dills, W.L., Jr.; Chen, P.; Baillargeon, B.M.; Westgate, C.L.
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Activity-based metabolomic profiling of enzymatic function: identification of Rv1248c as a mycobacterial 2-hydroxy-3-oxoadipate synthase
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Mycobacterium tuberculosis (P9WIS5), Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv (P9WIS5)
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Zhao, H.; de Carvalho, L.P.; Nathan, C.; Ouerfelli, O.
A protecting group-free synthesis of deazathiamine: a step toward inhibitor design
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Mycobacterium tuberculosis
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Balakrishnan, A.; Jordan, F.; Nathan, C.F.
Influence of allosteric regulators on individual steps in the reaction catalyzed by Mycobacterium tuberculosis 2-hydroxy-3-oxoadipate synthase
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Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv
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Patel, H.; Shim, D.; Farinas, E.; Jordan, F.
Investigation of the donor and acceptor range for chiral carboligation catalyzed by the E1 component of the 2-oxoglutarate dehydrogenase complex
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Escherichia coli (P0AFG3)
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Maksymiuk, C.; Ioerger, T.; Balakrishnan, A.; Bryk, R.; Rhee, K.; Sacchettini, J.; Nathan, C.
Comparison of transposon and deletion mutants in Mycobacterium tuberculosis The case of rv1248c, encoding 2-hydroxy-3-oxoadipate synthase
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Mycobacterium tuberculosis, Mycobacterium tuberculosis H37Rv, Mycobacterium tuberculosis CDC1551
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Wagner, T.; Andre-Leroux, G.; Hindie, V.; Barilone, N.; Lisa, M.N.; Hoos, S.; Raynal, B.; Vulliez-Le Normand, B.; OHare, H.M.; Bellinzoni, M.; Alzari, P.M.
Structural insights into the functional versatility of an FHA domain protein in mycobacterial signaling
Sci. Signal.
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eaav9504
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Mycolicibacterium smegmatis (A0R2B1), Mycolicibacterium smegmatis ATCC 700084 (A0R2B1)
brenda
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