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BRENDA KEGG MetaCyc

citric acid cycle (BRENDA)

:= BRENDA, := KEGG, := MetaCyc, := SABIO-RK
:= amino acid sequences := show the reaction diagram
EC Number
Reaction
Pathways
Reaction IDs
Stoichiometry Check
Missing Substrate
Missing Product
Commentary
Remark
2-oxoglutarate dehydrogenase system
2-oxoglutarate + CoA + NAD+ = succinyl-CoA + CO2 + NADH
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: multienzyme system: ec 1.2.4.2, ec 2.3.1.61 and ec 1.8.1.4 multi-step reaction (see R01700+R02570+R07618)
: This reaction sums up the three reactions that are catalyzed by the 2-oxoglutarate dehydrogenase complex.
natural substrates, multi-step reaction
1.2.1.ak
2-oxoglutarate + CoA + NAD+ = succinyl-CoA + CO2 + NADH
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: multienzyme system: ec 1.2.4.2, ec 2.3.1.61 and ec 1.8.1.4 multi-step reaction (see R01700+R02570+R07618)
: This reaction sums up the three reactions that are catalyzed by the 2-oxoglutarate dehydrogenase complex.
natural substrates, multi-step reaction
oxoglutarate dehydrogenase (succinyl-transferring)
2-oxoglutarate + CoA + NAD+ = succinyl-CoA + CO2 + NADH
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: multienzyme system: ec 1.2.4.2, ec 2.3.1.61 and ec 1.8.1.4 multi-step reaction (see R01700+R02570+R07618)
: This reaction sums up the three reactions that are catalyzed by the 2-oxoglutarate dehydrogenase complex.
natural substrates, multi-step reaction
3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring)
2-oxoglutarate + CoA + NAD+ = succinyl-CoA + CO2 + NADH
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: multienzyme system: ec 1.2.4.2, ec 2.3.1.61 and ec 1.8.1.4 multi-step reaction (see R01700+R02570+R07618)
: This reaction sums up the three reactions that are catalyzed by the 2-oxoglutarate dehydrogenase complex.
natural substrates, multi-step reaction
citrate (Si)-synthase
acetyl-CoA + H2O + oxaloacetate = citrate + CoA
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: (pro-S)-carboxymethyl-forming (ec 2.3.3.1) (pro-R)-carboxymethyl-forming (ec 2.3.3.3) unknown stereospecificity (ec 2.3.3.16)
: Citrate synthase is located solely in the mitochondrial matrix. Citrate enters the mitochondrial matrix to react with the enzyme. Experiments done in rat liver indicate that this reaction is physiologically irreversible [7060582]. The reaction occurs in peroxisome in fungi [1897942] and plants [15923350] and in bacterial cytosol[4211224]; Citrate synthase is located solely in the mitochondrial matrix. Citrate enters the mitochondrial matrix to react with the enzyme. Experiments done in rat liver indicate that this reaction is physiologically irreversible [7060582].
natural substrates
homocitrate synthase
acetyl-CoA + H2O + oxaloacetate = citrate + CoA
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: (pro-S)-carboxymethyl-forming (ec 2.3.3.1) (pro-R)-carboxymethyl-forming (ec 2.3.3.3) unknown stereospecificity (ec 2.3.3.16)
: Citrate synthase is located solely in the mitochondrial matrix. Citrate enters the mitochondrial matrix to react with the enzyme. Experiments done in rat liver indicate that this reaction is physiologically irreversible [7060582]. The reaction occurs in peroxisome in fungi [1897942] and plants [15923350] and in bacterial cytosol[4211224]; Citrate synthase is located solely in the mitochondrial matrix. Citrate enters the mitochondrial matrix to react with the enzyme. Experiments done in rat liver indicate that this reaction is physiologically irreversible [7060582].
natural substrates
citrate synthase (unknown stereospecificity)
acetyl-CoA + H2O + oxaloacetate = citrate + CoA
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: (pro-S)-carboxymethyl-forming (ec 2.3.3.1) (pro-R)-carboxymethyl-forming (ec 2.3.3.3) unknown stereospecificity (ec 2.3.3.16)
: Citrate synthase is located solely in the mitochondrial matrix. Citrate enters the mitochondrial matrix to react with the enzyme. Experiments done in rat liver indicate that this reaction is physiologically irreversible [7060582]. The reaction occurs in peroxisome in fungi [1897942] and plants [15923350] and in bacterial cytosol[4211224]; Citrate synthase is located solely in the mitochondrial matrix. Citrate enters the mitochondrial matrix to react with the enzyme. Experiments done in rat liver indicate that this reaction is physiologically irreversible [7060582].
natural substrates
citrate (Re)-synthase
acetyl-CoA + H2O + oxaloacetate = citrate + CoA
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: (pro-S)-carboxymethyl-forming (ec 2.3.3.1) (pro-R)-carboxymethyl-forming (ec 2.3.3.3) unknown stereospecificity (ec 2.3.3.16)
: Citrate synthase is located solely in the mitochondrial matrix. Citrate enters the mitochondrial matrix to react with the enzyme. Experiments done in rat liver indicate that this reaction is physiologically irreversible [7060582]. The reaction occurs in peroxisome in fungi [1897942] and plants [15923350] and in bacterial cytosol[4211224]; Citrate synthase is located solely in the mitochondrial matrix. Citrate enters the mitochondrial matrix to react with the enzyme. Experiments done in rat liver indicate that this reaction is physiologically irreversible [7060582].
natural substrates
citrate CoA-transferase
acetyl-CoA + citrate = acetate + (3S)-citryl-CoA
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natural substrates
succinate + FAD = fumarate + FADH2
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natural substrates
fumarate reductase (NADH)
succinate + FAD = fumarate + FADH2
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natural substrates
succinate dehydrogenase
succinate + FAD = fumarate + FADH2
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natural substrates
citryl-CoA lyase
(3S)-citryl-CoA = acetyl-CoA + oxaloacetate
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: a part of multi-step reaction (see R00352, R01322+R00354)
natural substrates
succinyl-CoA:acetate CoA-transferase
succinyl-CoA + acetoacetate = succinate + acetoacetyl-CoA
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natural substrates
3-oxoacid CoA-transferase
succinyl-CoA + acetoacetate = succinate + acetoacetyl-CoA
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natural substrates
ATP citrate synthase
ADP + phosphate + acetyl-CoA + oxaloacetate = ATP + citrate + CoA
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: multi-step reaction (see R01322+R00354)
natural substrates, multi-step reaction
malate dehydrogenase (quinone)
(S)-malate + a quinone = oxaloacetate + reduced quinone
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natural substrates
malate dehydrogenase (quinone)
(S)-malate + acceptor = oxaloacetate + reduced acceptor
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natural substrates, generic
succinate-CoA ligase (GDP-forming)
GTP + succinate + CoA = GDP + phosphate + succinyl-CoA
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natural substrates
citrate-CoA ligase
ATP + citrate + CoA = ADP + phosphate + (3S)-citryl-CoA
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: a part of multi-step reaction (see R00352, R01322+R00354)
natural substrates