Information on EC 2.2.1.5 - 2-hydroxy-3-oxoadipate synthase

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

EC NUMBER
COMMENTARY
2.2.1.5
-
RECOMMENDED NAME
GeneOntology No.
2-hydroxy-3-oxoadipate synthase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
2-oxoglutarate + glyoxylate = 2-hydroxy-3-oxoadipate + CO2
show the reaction diagram
mechanism
-
2-oxoglutarate + glyoxylate = 2-hydroxy-3-oxoadipate + CO2
show the reaction diagram
various alternative mechanisms proposed
-
2-oxoglutarate + glyoxylate = 2-hydroxy-3-oxoadipate + CO2
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
decarboxylation
-
-
synergistic
-
PATHWAY
KEGG Link
MetaCyc Link
Glyoxylate and dicarboxylate metabolism
-
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.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
2-hydroxy-3-oxoadipate glyoxylate-lyase (carboxylating)
-
-
-
-
2-hydroxy-3-oxoadipate synthase
O50463
-
2-oxoglutarate: glyoxylate carboligase
-
-
-
-
alpha-ketoglutarate:glyoxylate carboligase
-
-
-
-
alpha-ketoglutaric-glyoxylic carboligase
-
-
-
-
carboligase
-
-
-
-
carboligase
O50463
-
EC 4.1.3.15
-
-
formerly
-
glyoxylate-2-oxoglutarate carboligase
-
-
-
-
HOA synthase
O50463
-
oxoglutarate: glyoxylate carboligase
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9054-72-2
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
commercial preparation
-
-
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
pig
-
-
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
? + CO2
show the reaction diagram
-
-
-
-
2-oxoglutarate
? + CO2
show the reaction diagram
-
decarboxylation
-
-
-
2-oxoglutarate
? + CO2
show the reaction diagram
-
identical with 2-oxoglutarate decarboxylase
-
-
-
2-oxoglutarate + acetaldehyde
5-hydroxy-4-oxohexanoate + CO2
show the reaction diagram
-
-
-
-
-
2-oxoglutarate + acetaldehyde
5-hydroxy-4-oxohexanoate + CO2
show the reaction diagram
-
-
-
-
-
2-oxoglutarate + acetaldehyde
5-hydroxy-4-oxohexanoate + CO2
show the reaction diagram
-
-
-
-
2-oxoglutarate + glyoxylate
2-hydroxy-3-oxohexandioate + CO2
show the reaction diagram
-
-
-
-
-
2-oxoglutarate + glyoxylate
2-hydroxy-3-oxohexandioate + CO2
show the reaction diagram
-
-
-
-
2-oxoglutarate + glyoxylate
2-hydroxy-3-oxohexandioate + CO2
show the reaction diagram
-
-
-
-
-
2-oxoglutarate + glyoxylate
2-hydroxy-3-oxohexandioate + CO2
show the reaction diagram
-
-
-
-
-
2-oxoglutarate + glyoxylate
2-hydroxy-3-oxohexandioate + CO2
show the reaction diagram
-
-
-
-
-
2-oxoglutarate + glyoxylate
2-hydroxy-3-oxohexandioate + CO2
show the reaction diagram
-
-
-
-
-
2-oxoglutarate + glyoxylate
2-hydroxy-3-oxohexandioate + CO2
show the reaction diagram
-
-
-
-
-
2-oxoglutarate + glyoxylate
2-hydroxy-3-oxohexandioate + CO2
show the reaction diagram
-
-
i. e. 2-hydroxy-3-oxoadipic acid
-
2-oxoglutarate + glyoxylate
2-hydroxy-3-oxohexandioate + CO2
show the reaction diagram
-
-
i. e. 2-hydroxy-3-oxoadipic acid
-
2-oxoglutarate + glyoxylate
2-hydroxy-3-oxohexandioate + CO2
show the reaction diagram
-
-
also 2,3-dihydroxy-4-ketopimelic acid
-
2-oxoglutarate + glyoxylate
2-hydroxy-3-oxohexandioate + CO2
show the reaction diagram
-
-
further spontaneous decarboxylation in the presence of acid
-
2-oxoglutarate + glyoxylate
2-hydroxy-3-oxohexandioate + CO2
show the reaction diagram
-
-
further spontaneous decarboxylation in the presence of acid
-
2-oxoglutarate + glyoxylate
2-hydroxy-3-oxohexandioate + CO2
show the reaction diagram
-
-
further decarboxylation leads to 5-hydroxy-4-ketovaleric acid
-
2-oxoglutarate + glyoxylate
?
show the reaction diagram
-
linked to citric acid cycle
-
-
-
2-oxoglutarate + glyoxylate
?
show the reaction diagram
-
possible 1-carbon source for nicotine synthesis
-
-
-
2-oxoglutarate + glyoxylate
?
show the reaction diagram
-
hypothesized 2-oxoglutarate regeneration cycle
-
-
-
2-oxoglutarate + glyoxylate
?
show the reaction diagram
-
important as diversion of glyoxylate from oxalate formation
-
-
-
2-oxoglutarate + glyoxylate
2-hydroxy-3-oxoadipate + CO2
show the reaction diagram
-
-
-
-
?
2-oxoglutarate + glyoxylate
2-hydroxy-3-oxoadipate + CO2
show the reaction diagram
O50463
-
-
-
?
additional information
?
-
O50463
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), 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, 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
-
-
-
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
2-oxoglutarate + glyoxylate
?
show the reaction diagram
-
linked to citric acid cycle
-
-
-
2-oxoglutarate + glyoxylate
?
show the reaction diagram
-
possible 1-carbon source for nicotine synthesis
-
-
-
2-oxoglutarate + glyoxylate
?
show the reaction diagram
-
hypothesized 2-oxoglutarate regeneration cycle
-
-
-
2-oxoglutarate + glyoxylate
?
show the reaction diagram
-
important as diversion of glyoxylate from oxalate formation
-
-
-
additional information
?
-
O50463
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), 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
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
thiamine diphosphate
-
-
thiamine diphosphate
-
-
thiamine diphosphate
-
-
thiamine diphosphate
-
-
thiamine diphosphate
-
-
thiamine diphosphate
-
-
thiamine diphosphate
-
-
thiamine diphosphate
-
deficiency may lead to hyperoxaluria and glyoxylate excretion
thiamine diphosphate
-
-
thiamine diphosphate
O50463
strictly dependent on
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Cl-
-
stimulates
Mg2+
-
31% activation at 1 mM
Mg2+
-
Mg2+-deficient food leads to 27-35% loss of activity in vivo
Mg2+
O50463
strictly dependent on
Mn2+
-
substitutes for Mg2+
Mn2+
-
175% activation at 1 mM
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
deazathiamine diphosphate
-
binds 32fold more tightly to the enzyme than thiamine diphosphate
-
EDTA
-
93% inhibition at 1 mM
EDTA
-
complete inhibition at 10 mM
iodoacetic acid
-
83% inhibition at 3.3 mM
N-ethylmaleimide
-
74% inhibition at 0.01 mM
p-Chloromercuriphenylsulfonic acid
-
complete inhibition at 1 mM
Zn2+
-
97% inhibition at 1 mM
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
Avidin
-
-
-
mercaptoethanol
-
stimulates
perchloric acid
-
-
Sucrose
-
stimulates
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1.8
-
2-oxoglutarate
-
-
2
-
2-oxoglutarate
-
-
16
-
2-oxoglutarate
-
-
3.2
-
glyoxylate
-
-
3.6
-
glyoxylate
-
-
6.8
-
glyoxylate
-
-
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.144
-
deazathiamine
-
pH not specified in the publication, temperature not specified in the publication
0.0067
-
deazathiamine diphosphate
-
pH not specified in the publication, temperature not specified in the publication
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.128
-
-
maximum, cell-cycle-dependent
0.8
-
-
-
85
-
-
-
additional information
-
-
-
additional information
-
-
thiamine deficiency decreases specific activity
additional information
-
-
assay method using high pressure liquid chromatography
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.5
-
-
enzyme assay at
6.5
-
-
enzyme assay at
7
-
-
enzyme assay at
7
-
-
enzyme assay at
7
-
-
-
7
-
-
enzyme assay at
7.1
-
-
enzyme assay at
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
7.5
-
-
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
-
-
enzyme assay at
30
-
-
enzyme assay at
37
-
-
enzyme assay at
37
-
-
enzyme assay at
37
-
-
enzyme assay at
37
-
-
enzyme assay at
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
part of alpha-ketoglutarate dehydrogenase complex
Manually annotated by BRENDA team
-
exclusively; part of alpha-ketoglutarate dehydrogenase complex
Manually annotated by BRENDA team
-
part of alpha-ketoglutarate dehydrogenase complex
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
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)
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)
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
47
-
-
50% loss of activity after 3 min
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
mercaptoethanol stabilises
-
Mg2+ stabilises
-
sucrose stabilises
-
OXIDATION STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
access of air destabilises
-
395930
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20°C, potassium phosphate buffer, pH 7.1, 10% glycerol, 1 mM dithiothreitol, at least several days
-
-20°C, potassium phosphate buffer, pH 7.0, 5 days
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
partial
-
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
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%