Information on EC 6.2.1.8 - oxalate-CoA ligase

for references in articles please use BRENDA:EC6.2.1.8
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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
6.2.1.8
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RECOMMENDED NAME
GeneOntology No.
oxalate-CoA ligase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + oxalate + CoA = AMP + diphosphate + oxalyl-CoA
show the reaction diagram
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acid-thiol ligation
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
oxalate degradation VI
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Glyoxylate and dicarboxylate metabolism
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Metabolic pathways
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SYSTEMATIC NAME
IUBMB Comments
oxalate:CoA ligase (AMP-forming)
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CAS REGISTRY NUMBER
COMMENTARY hide
37318-57-3
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Cajanus indicus
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Manually annotated by BRENDA team
chick-pea
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
Lens sp.
lentil
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Manually annotated by BRENDA team
Lupinus sp.
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Manually annotated by BRENDA team
ecotype R108
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Manually annotated by BRENDA team
cultivar Zhonghua 11
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Manually annotated by BRENDA team
Pumpkin
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Manually annotated by BRENDA team
gene YBR222C
UniProt
Manually annotated by BRENDA team
gene YBR222C
UniProt
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + oxalate + CoA
?
show the reaction diagram
ATP + oxalate + CoA
AMP + diphosphate + oxalyl-CoA
show the reaction diagram
CTP + oxalate + CoA
CMP + diphosphate + oxalyl-CoA
show the reaction diagram
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at 15% the activity relative to ATP
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GTP + oxalate + CoA
GMP + diphosphate + oxalyl-CoA
show the reaction diagram
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at 6% of the actvity relative to ATP
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UTP + oxalate + CoA
UMP + diphosphate + oxalyl-CoA
show the reaction diagram
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at 21% the activity relative to ATP
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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
ATP + oxalate + CoA
?
show the reaction diagram
ATP + oxalate + CoA
AMP + diphosphate + oxalyl-CoA
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1-ethyl-3-(3-dimethylaminopropyl)carbodiimide
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almost complete inhibition at 5 mM
5'-dithiobis-(2-nitrobenzoic acid)
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less than 10% residual activity at 0.1 mM
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hydroxylamine
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inhibition of ATP-diphosphate exchange
MgCl2
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high concentrations cause a marked inhibition of ATP-diphosphate exchange
N-ethylmaleimide
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complete inhibition in Tris-HCl at 0.1 mM
NaF
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slight inhibition of ATP-diphosphate exchange
oxalate
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high concentrations cause a slight inhibition of ATP-diphosphate exchange
PCMB
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inhibition of ATP-diphosphate exchange. Reversal of inhibition by GSH or cysteine
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4
ATP
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0.1
CoA
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0.02 - 44.5
oxalate
additional information
additional information
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.4
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ATP-diphosphate exchange
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 10
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activity range, profile overview
6 - 10
activity range, profile overview
6.3 - 8.6
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6.3: about 60% of maximal activity, 8.6: about 50% of maximal activity, ATP-diphosphate exchange
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
apo, ATP-bound, as well as oxalate- and AMP-bound enzyme states, hanging drop vapor diffusion method, using
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
3 enzyme forms: OCS-1, OCS-2 and OCS-3
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HisTrap column chromatography
Ni-NTA column chromatography and Sephadex G-25 gel filtration
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nickel chelating affinity column chromatography
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recombinant His-tagged enzyme from Escherichia coli strain BLR(DE3) by nickel affinity chromatography to over 90% purity
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
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expressed in Escherichia coli BLR(DE3) cells and Nicotiana tabacum leaves
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expression of GFP-tagged enzyme in onion epidermal cell cytoplasm using the constitutive 35S promoter, and from binary construct, transfected into Agrobacterium tumefaciens, GFP-tagged enzyme is transiently expressed in Nicotiana benthamiana leaf cytoplasm
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gene YBR222C, expression of His-tagged enzyme in Escherichia coli strain BLR(DE3)
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
exogenous application of oxalate results in enzyme expression induction. Enzyme expression in rice bean root tips is enhanced greatly by aluminium stress (0.025-0.05 mM)
oxalate induced the enzyme, quantitative RT-PCR reveals that ScAAE3 transcript levels are induced within min of exposure peaking at about 1 h before declining back to steady state levels
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H214A
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the mutant shows strongly reduced activity compared to the wild type enzyme
H319A
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the mutant shows strongly reduced activity compared to the wild type enzyme
K500A
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the mutant shows strongly reduced activity compared to the wild type enzyme
R409A
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the mutant shows strongly reduced activity compared to the wild type enzyme
S289A
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the mutant shows strongly reduced activity compared to the wild type enzyme
C219G
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the mutant shows 5.6% activity compared to the wild type enzyme
C287G
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the mutant shows 25.4% activity compared to the wild type enzyme
C363G
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the mutant shows 7.2% activity compared to the wild type enzyme
C454G
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the mutant shows 44.5% activity compared to the wild type enzyme
C473G
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the mutant shows 42.9% activity compared to the wild type enzyme
additional information
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aae3-1 and aae3-2 are null mutants are deficient in oxalyl-CoA synthetase