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ATP + oxalate + CoA
AMP + diphosphate + oxalyl-CoA
CTP + oxalate + CoA
CMP + diphosphate + oxalyl-CoA
-
Substrates: at 15% the activity relative to ATP
Products: -
?
GTP + oxalate + CoA
GMP + diphosphate + oxalyl-CoA
-
Substrates: at 6% of the activity relative to ATP
Products: -
?
UTP + oxalate + CoA
UMP + diphosphate + oxalyl-CoA
-
Substrates: at 21% the activity relative to ATP
Products: -
?
additional information
?
-
ATP + oxalate + CoA

?
-
Substrates: key enzyme in the biosynthesis of beta-oxalyl amino alanine
Products: -
?
ATP + oxalate + CoA
?
-
Substrates: key enzyme in the biosynthesis of beta-oxalyl amino alanine
Products: -
?
ATP + oxalate + CoA

AMP + diphosphate + oxalyl-CoA
Substrates: -
Products: -
?
ATP + oxalate + CoA
AMP + diphosphate + oxalyl-CoA
Substrates: specific for oxalate
Products: -
?
ATP + oxalate + CoA
AMP + diphosphate + oxalyl-CoA
Substrates: oxalate is the specific substrate
Products: -
?
ATP + oxalate + CoA
AMP + diphosphate + oxalyl-CoA
-
Substrates: -
Products: -
?
ATP + oxalate + CoA
AMP + diphosphate + oxalyl-CoA
-
Substrates: highly specific for oxalate
Products: -
?
ATP + oxalate + CoA
AMP + diphosphate + oxalyl-CoA
-
Substrates: -
Products: -
?
ATP + oxalate + CoA
AMP + diphosphate + oxalyl-CoA
Substrates: -
Products: -
?
ATP + oxalate + CoA
AMP + diphosphate + oxalyl-CoA
-
Substrates: -
Products: -
?
ATP + oxalate + CoA
AMP + diphosphate + oxalyl-CoA
-
Substrates: -
Products: -
?
ATP + oxalate + CoA
AMP + diphosphate + oxalyl-CoA
-
Substrates: the enzyme is highly specific for oxalate
Products: -
?
ATP + oxalate + CoA
AMP + diphosphate + oxalyl-CoA
Substrates: -
Products: -
?
ATP + oxalate + CoA
AMP + diphosphate + oxalyl-CoA
Substrates: -
Products: -
?
ATP + oxalate + CoA
AMP + diphosphate + oxalyl-CoA
-
Substrates: -
Products: -
?
ATP + oxalate + CoA
AMP + diphosphate + oxalyl-CoA
Substrates: oxalate is the specific substrate
Products: -
?
additional information

?
-
Substrates: no activity with malonate, succinate, malate, acetate, formate, lactate, glycolate, glyoxylate, and glutarate
Products: -
?
additional information
?
-
-
Substrates: no activity with malonate, succinate, malate, acetate, formate, lactate, glycolate, glyoxylate, and glutarate
Products: -
?
additional information
?
-
-
Substrates: enzyme catalyzes oxalate-dependent and CoA-independent ATP-diphosphate exchange
Products: -
?
additional information
?
-
Substrates: the enzyme's catalytic efficiency for malonate and the activity with succinate is bellow detection limit. The enzyme shows no activity with succinate, glycolate, and lactate
Products: -
?
additional information
?
-
-
Substrates: no activity with malonate, succinate, malate, acetate, formate, lactate, glycolate, and glyoxylate
Products: -
?
additional information
?
-
Substrates: no activity with malonate, succinate, malate, formate, acetate, lactate, glycolate, and glutarate
Products: -
?
additional information
?
-
-
Substrates: no activity with malonate, succinate, malate, formate, acetate, lactate, glycolate, and glutarate
Products: -
?
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ATP + oxalate + CoA
AMP + diphosphate + oxalyl-CoA
ATP + oxalate + CoA

?
-
Substrates: key enzyme in the biosynthesis of beta-oxalyl amino alanine
Products: -
?
ATP + oxalate + CoA
?
-
Substrates: key enzyme in the biosynthesis of beta-oxalyl amino alanine
Products: -
?
ATP + oxalate + CoA

AMP + diphosphate + oxalyl-CoA
Substrates: -
Products: -
?
ATP + oxalate + CoA
AMP + diphosphate + oxalyl-CoA
Substrates: oxalate is the specific substrate
Products: -
?
ATP + oxalate + CoA
AMP + diphosphate + oxalyl-CoA
-
Substrates: -
Products: -
?
ATP + oxalate + CoA
AMP + diphosphate + oxalyl-CoA
Substrates: -
Products: -
?
ATP + oxalate + CoA
AMP + diphosphate + oxalyl-CoA
-
Substrates: -
Products: -
?
ATP + oxalate + CoA
AMP + diphosphate + oxalyl-CoA
-
Substrates: the enzyme is highly specific for oxalate
Products: -
?
ATP + oxalate + CoA
AMP + diphosphate + oxalyl-CoA
Substrates: -
Products: -
?
ATP + oxalate + CoA
AMP + diphosphate + oxalyl-CoA
Substrates: -
Products: -
?
ATP + oxalate + CoA
AMP + diphosphate + oxalyl-CoA
-
Substrates: -
Products: -
?
ATP + oxalate + CoA
AMP + diphosphate + oxalyl-CoA
Substrates: oxalate is the specific substrate
Products: -
?
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additional information
additional information
-
0.02
oxalate

pH 7.5, temperature not specified in the publication
0.04215
oxalate
pH and temperature not specified in the publication
0.0715
oxalate
at pH 8.0 and 25°C
0.081
oxalate
-
at pH 8.0, temperature not specified in the publication
0.1051
oxalate
-
at pH 8.0, temperature not specified in the publication
0.121
oxalate
at pH 4.5 and 25°C
0.149
oxalate
pH 8.0, temperature not specified in the publication
0.2238
oxalate
-
isoform AAE3-1, at pH 8.0, temperature not specified in the publication
1.73
oxalate
-
wild type enzyme, at pH 7.5 and 37°C
2.62
oxalate
-
mutant enzyme C473G, at pH 7.5 and 37°C
3.82
oxalate
-
mutant enzyme C219G, at pH 7.5 and 37°C
4.64
oxalate
-
mutant enzyme C363G, at pH 7.5 and 37°C
44.5
oxalate
-
mutant enzyme C454G, at pH 7.5 and 37°C
additional information
additional information

Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
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malfunction

a Scaae3 deletion mutant strain shows highly reduced oxalate degradation activity decreasing recovery from exposure to oxalate, e.g. by exposure to oxalate-secreting microbes, and to oxidative stress, e.g. by H2O2
malfunction
aae3 null mutants show increased soluble and insoluble oxalate contents compared to the wild-type enzyme, loss of AAE3 interferes with seed development affecting the integrity and function of the seed coat, phenotype, overview
malfunction
-
reduction of enzyme expression increases susceptibility of Medicago truncatula to the oxalate-secreting fungal pathogen Sclerotinia sclerotiorum and results in the accumulation of druse crystals of calcium oxalate
malfunction
-
enzyme knockout of isoform AAE3-1 improves tomato fruit quality, resulting in higher total sugar content and lower total acid content
malfunction
-
a Scaae3 deletion mutant strain shows highly reduced oxalate degradation activity decreasing recovery from exposure to oxalate, e.g. by exposure to oxalate-secreting microbes, and to oxidative stress, e.g. by H2O2
-
metabolism

the enzyme catalyzes the first step in oxalate degradation
metabolism
-
the enzyme is involved in oxalate catabolism
physiological function

the enzyme catalyzes the first step in a pathway of oxalate degradation to protect the cell against the harmful effects of oxalate derived from an endogenous process or an environmental source
physiological function
oxalyl-CoA synthetase is required for oxalate degradation, for normal seed development, and for defense against an oxalate-producing fungal pathogen, e.g. the fungus Sclerotinia sclerotiorum
physiological function
the enzyme is involved in aluminum tolerance
physiological function
enzyme-dependent degradation of oxalate is important for normal seed development and for defense against oxalate-producing fungal pathogens
physiological function
-
enzyme overexpression increases cadmium and aluminium tolerances in Arabidopsis thaliana and soybean hairy roots, which is associated with a decrease in oxalate accumulation
physiological function
-
the enzyme catalyzes the first step in a pathway of oxalate degradation to protect the cell against the harmful effects of oxalate derived from an endogenous process or an environmental source
-
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H214A
the mutant shows strongly reduced activity compared to the wild type enzyme
H319A
the mutant shows strongly reduced activity compared to the wild type enzyme
K500A
the mutant shows strongly reduced activity compared to the wild type enzyme
R409A
the mutant shows strongly reduced activity compared to the wild type enzyme
S289A
the mutant shows strongly reduced activity compared to the wild type enzyme
C219G
-
the mutant shows 5.6% activity compared to the wild type enzyme
C287G
-
the mutant shows 25.4% activity compared to the wild type enzyme
C363G
-
the mutant shows 7.2% activity compared to the wild type enzyme
C454G
-
the mutant shows 44.5% activity compared to the wild type enzyme
C473G
-
the mutant shows 42.9% activity compared to the wild type enzyme
additional information

aae3-1 and aae3-2 are null mutants are deficient in oxalyl-CoA synthetase
additional information
-
aae3-1 and aae3-2 are null mutants are deficient in oxalyl-CoA synthetase
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Adsule, R.N.; Barat, G.K.
Occurrence of oxalyl-CoA synthetase in Indian pulses
Experientia
33
416-417
1977
Lathyrus sativus, Lathyrus oleraceus, Lens sp., Cicer arietinum, Cajanus indicus, Glycine max, Vigna radiata var. radiata, Vigna unguiculata subsp. unguiculata
brenda
Sehgal, D.; Santha, I.M.; Mehta, S.L.
Purification of oxalyl CoA synthetase enzyme from Lathyrus sativus and raising of antibodies
J. Plant Biochem. Biotechnol.
1
97-100
1992
Lathyrus sativus, Lathyrus sativus P-24
-
brenda
Giovanelli, J.
Oxalyl-coenzyme A synthetase from pea seed
Biochim. Biophys. Acta
118
124-143
1966
Lathyrus oleraceus, Lupinus sp., Pumpkin, Triticum aestivum
brenda
Foster, J.; Nakata, P.A.
An oxalyl-CoA synthetase is important for oxalate metabolism in Saccharomyces cerevisiae
FEBS Lett.
588
160-166
2014
Saccharomyces cerevisiae (P38137), Saccharomyces cerevisiae, Saccharomyces cerevisiae BY4741 (P38137)
brenda
Foster, J.; Kim, H.U.; Nakata, P.A.; Browse, J.
A previously unknown oxalyl-CoA synthetase is important for oxalate catabolism in Arabidopsis
Plant Cell
24
1217-1229
2012
Arabidopsis thaliana (Q9SMT7), Arabidopsis thaliana
brenda
Fan, M.; Xiao, Y.; Li, M.; Chang, W.
Crystal structures of Arabidopsis thaliana oxalyl-CoA synthetase essential for oxalate degradation
Mol. Plant
9
1349-1352
2016
Arabidopsis thaliana (Q9SMT7), Arabidopsis thaliana
brenda
Peng, C.; Liang, X.; Liu, E.E.; Zhang, J.J.; Peng, X.X.
The oxalyl-CoA synthetase-regulated oxalate and its distinct effects on resistance to bacterial blight and aluminium toxicity in rice
Plant Biol.
19
345-353
2017
Oryza sativa
brenda
Lou, H.Q.; Fan, W.; Xu, J.M.; Gong, Y.L.; Jin, J.F.; Chen, W.W.; Liu, L.Y.; Hai, M.R.; Yang, J.L.; Zheng, S.J.
An oxalyl-CoA synthetase is involved in oxalate degradation and aluminum tolerance
Plant Physiol.
172
1679-1690
2016
Vigna umbellata (A0A1C9HM85), Vigna umbellata
brenda
Foster, J.; Luo, B.; Nakata, P.A.
An oxalyl-CoA dependent pathway of oxalate catabolism plays a role in regulating calcium oxalate crystal accumulation and defending against oxalate-secreting phytopathogens in Medicago truncatula
PLoS ONE
11
e0149850
2016
Medicago truncatula
brenda
Li, P.; He, Q.; Jin, J.; Liu, Y.; Wen, Y.; Zhao, K.; Mao, G.; Fan, W.; Yang, J.
Tomato oxalyl-CoA synthetase degrades oxalate and affects fruit quality
Front. Plant Sci.
13
951386
2022
Solanum lycopersicum
brenda
Xian, P.; Cai, Z.; Cheng, Y.; Lin, R.; Lian, T.; Ma, Q.; Nian, H.
Wild soybean oxalyl-CoA synthetase degrades oxalate and affects the tolerance to cadmium and aluminum stresses
Int. J. Mol. Sci.
21
8869
2020
Glycine soja
brenda
Goldsmith, M.; Barad, S.; Peleg, Y.; Albeck, S.; Dym, O.; Brandis, A.; Mehlman, T.; Reich, Z.
The identification and characterization of an oxalyl-CoA synthetase from grass pea (Lathyrus sativus L.)
RSC Chem. Biol.
3
320-333
2022
Lathyrus sativus (A0A858C9Q9)
brenda