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FGROUP
SUBSTRUCTURE
compound
enzyme
Multiple
keto-Oxaloacetate
Enzyme(s) or Pathway(s)
1.1.1.37
malate dehydrogenase
1.1.1.82
malate dehydrogenase (NADP+)
1.1.3.3
malate oxidase
1.1.99.16
malate dehydrogenase (acceptor)
1.1.99.7
lactate-malate transhydrogenase
1.4.1.21
aspartate dehydrogenase
1.4.3.1
D-aspartate oxidase
1.4.3.16
L-aspartate oxidase
2.1.3.1
methylmalonyl-CoA carboxytransferase
2.3.3.1
citrate (Si)-synthase
2.3.3.2
decylcitrate synthase
2.3.3.3
citrate (Re)-synthase
2.3.3.5
2-methylcitrate synthase
2.3.3.8
ATP citrate synthase
2.6.1.1
aspartate transaminase
2.6.1.31
pyridoxamine-oxaloacetate transaminase
2.6.1.35
glycine-oxaloacetate transaminase
2.6.1.70
aspartate-phenylpyruvate transaminase
2.6.1.78
aspartate---prephenate aminotransferase
3.1.1.44
4-methyloxaloacetate esterase
3.7.1.1
oxaloacetase
4.1.1.3
oxaloacetate decarboxylase
4.1.1.31
phosphoenolpyruvate carboxylase
4.1.1.32
phosphoenolpyruvate carboxykinase (GTP)
4.1.1.38
phosphoenolpyruvate carboxykinase (diphosphate)
4.1.1.49
phosphoenolpyruvate carboxykinase (ATP)
4.1.3.13
oxalomalate lyase
4.1.3.34
citryl-CoA lyase
4.1.3.6
citrate (pro-3S)-lyase
4.2.1.32
L(+)-tartrate dehydratase
4.2.1.81
D(-)-tartrate dehydratase
4.3.1.16
threo-3-hydroxyaspartate ammonia-lyase
4.3.1.20
erythro-3-hydroxyaspartate ammonia-lyase
5.3.2.2
oxaloacetate tautomerase
6.4.1.1
pyruvate carboxylase
Structure Data
Molfile
InChI
Advanced COMPOUND page
Database Links
ChEBI:30744
KEGG:C00036
PubChem:3338
NCI:077688
BiSSCat v1.06.20
http://bisscat.org/
Developed by Masaaki Kotera, Department of Biochemistry, Trinity College Dublin.
Science Foundation of Ireland is gratefully acknowledged.