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 hide
2.2.1.5
-
RECOMMENDED NAME
GeneOntology No.
2-hydroxy-3-oxoadipate synthase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
2-oxoglutarate + glyoxylate = 2-hydroxy-3-oxoadipate + CO2
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
decarboxylation
-
-
synergistic
-
PATHWAY
BRENDA Link
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.
CAS REGISTRY NUMBER
COMMENTARY hide
9054-72-2
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
tobacco
-
-
Manually annotated by BRENDA team
rabbit
-
-
Manually annotated by BRENDA team
pig
-
-
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
? + CO2
show the reaction diagram
2-oxoglutarate + acetaldehyde
5-hydroxy-4-oxohexanoate + CO2
show the reaction diagram
2-oxoglutarate + ethyl glyoxylate
(R)-6-ethoxy-5-hydroxy-4,6-dioxohexanoic acid + CO2
show the reaction diagram
-
81% enantiomeric excess
-
?
2-oxoglutarate + glyoxylate
(R)-2-hydroxy-3-oxoadipate + CO2
show the reaction diagram
-
90% enantiomeric excess
-
?
2-oxoglutarate + glyoxylate
2-hydroxy-3-oxoadipate + CO2
show the reaction diagram
2-oxoglutarate + glyoxylate
2-hydroxy-3-oxohexandioate + CO2
show the reaction diagram
2-oxoglutarate + glyoxylate
?
show the reaction diagram
2-oxoglutarate + methylglyoxal
(R)-5-hydroxy-4,6-dioxoheptanoic acid + CO2
show the reaction diagram
-
83% enantiomeric excess
-
?
2-oxoisovalerate + ethyl glyoxylate
(S)-ethyl 2-hydroxy-4-methyl-3-oxopentanoic acid + CO2
show the reaction diagram
-
81% enantiomeric excess
-
?
2-oxoisovalerate + glyoxylate
(S)-2-hydroxy-4-methyl-3-oxopentanoic acid + CO2
show the reaction diagram
-
67% enantiomeric excess
-
?
2-oxoisovalerate + methylglyoxal
(S)-3-hydroxy-5-methylhexane-2,4-dione + CO2
show the reaction diagram
-
more than 90% enantiomeric excess
-
?
2-oxovalerate + ethyl glyoxylate
(S)-ethyl 2-hydroxy-3-oxohexanoic acid + CO2
show the reaction diagram
-
52% enantiomeric excess
-
?
2-oxovalerate + glyoxylate
(S)-2-hydroxy-3-oxohexanoic acid + CO2
show the reaction diagram
-
96% enantiomeric excess
-
?
2-oxovalerate + methylglyoxal
(S)-3-hydroxyheptane-2,4-dione + CO2
show the reaction diagram
-
81% enantiomeric excess
-
?
additional information
?
-
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 + glyoxylate
2-hydroxy-3-oxoadipate + CO2
show the reaction diagram
2-oxoglutarate + glyoxylate
?
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
thiamine diphosphate
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cl-
-
stimulates
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
deazathiamine diphosphate
-
binds 32fold more tightly to the enzyme than thiamine diphosphate
GarA protein
-
non-competitive inhibition
-
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
COMMENTARY hide
LITERATURE
IMAGE
Avidin
-
-
-
mercaptoethanol
-
stimulates
perchloric acid
-
-
Sucrose
-
stimulates
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.84 - 16
2-oxoglutarate
3.2 - 6.8
glyoxylate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4.25
2-oxoglutarate
Mycobacterium tuberculosis
-
at pH 6.5 and 37°C
5.29
glyoxylate
Mycobacterium tuberculosis
-
at pH 6.5 and 37°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5060
2-oxoglutarate
Mycobacterium tuberculosis
-
at pH 6.5 and 37°C
34
1653
glyoxylate
Mycobacterium tuberculosis
-
at pH 6.5 and 37°C
101
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.36
GarA protein
-
at pH 6.5 and 37°C
-
53.1
glyoxylate
-
at pH 6.5 and 37°C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
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
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.128
-
maximum, cell-cycle-dependent
0.8
-
-
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.1
-
enzyme assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 7.5
-
-
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
47
-
50% loss of activity after 3 min
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
mercaptoethanol stabilises
-
Mg2+ stabilises
-
sucrose stabilises
-
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
access of air destabilises
-
395930
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, potassium phosphate buffer, pH 7.0, 5 days
-
-20°C, potassium phosphate buffer, pH 7.1, 10% glycerol, 1 mM dithiothreitol, at least several days
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, Q Sepharose column chromatography, Mono Q column chromatography, and Sephacryl S-100 gel filtration
-
partial
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) CodonPlus-RILP cells
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
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