+ |
succinate(2-) | up-regulates quantity
precursor of
|
fumarate(2-) |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-266275 |
|
|
Homo sapiens |
|
pmid |
sentence |
16143825 |
Mitochondrial succinate dehydrogenase (SDH) consists merely of four nuclearly encoded subunits. It participates in the electron transfer in the respiratory chain and in succinate catabolism in the Krebs cycle. The SDH enzyme, also known as respiratory chain complex II, faces the mitochondrial matrix and is bound to the inner membrane. The human enzyme readily oxidizes succinate to fumarate, while the reverse reaction is hardly detectable in most human cells and tissues under standard conditions. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | Citric acid cycle |
+ |
Succinyl-CoA GTP variant | up-regulates quantity
chemical modification
|
succinate(2-) |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-266270 |
|
|
Homo sapiens |
|
pmid |
sentence |
27487822 |
In the citric acid cycle, succinyl-CoA synthetase (SCS) catalyzes the only step that provides substrate-level phosphorylation: succinyl-CoA + NDP + Pi = succinate + CoA + NTP, where N is adenosine or guanosine and the reaction requires magnesium ions. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | Citric acid cycle |
+ |
ALDH5A1 | up-regulates quantity
chemical modification
|
succinate(2-) |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-266617 |
|
|
Homo sapiens |
|
pmid |
sentence |
19300440 |
Succinic semialdehyde dehydrogenase (SSADH) is involved in the final degradation step of the inhibitory neurotransmitter gamma-aminobutyric acid by converting succinic semialdehyde to succinic acid in the mitochondrial matrix. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
BBOX1 | up-regulates quantity
chemical modification
|
succinate(2-) |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-269700 |
|
|
Homo sapiens |
|
pmid |
sentence |
11802770 |
In the last step, butyrobetaine is hydroxylated on the 3-position by γ-butyrobetaine dioxygenase (BBD; EC 1.14.11.1) to yield carnitine. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | Carnitine biosynthesis |
+ |
succinyl-CoA(5-) | up-regulates quantity
precursor of
|
succinate(2-) |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-266265 |
|
|
Homo sapiens |
|
pmid |
sentence |
27487822 |
In the citric acid cycle, succinyl-CoA synthetase (SCS) catalyzes the only step that provides substrate-level phosphorylation: succinyl-CoA + NDP + Pi = succinate + CoA + NTP, where N is adenosine or guanosine and the reaction requires magnesium ions. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-266266 |
|
|
Homo sapiens |
|
pmid |
sentence |
27487822 |
In the citric acid cycle, succinyl-CoA synthetase (SCS) catalyzes the only step that provides substrate-level phosphorylation: succinyl-CoA + NDP + Pi = succinate + CoA + NTP, where N is adenosine or guanosine and the reaction requires magnesium ions. |
|
Publications: |
2 |
Organism: |
Homo Sapiens |
Pathways: | Citric acid cycle |
+ |
4-oxobutanoate | up-regulates quantity
precursor of
|
succinate(2-) |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-266615 |
|
|
Homo sapiens |
|
pmid |
sentence |
19300440 |
Succinic semialdehyde dehydrogenase (SSADH) is involved in the final degradation step of the inhibitory neurotransmitter gamma-aminobutyric acid by converting succinic semialdehyde to succinic acid in the mitochondrial matrix. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
2-oxoglutarate(2-) | up-regulates quantity
precursor of
|
succinate(2-) |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-269686 |
|
|
Homo sapiens |
|
pmid |
sentence |
11431483 |
Epsilon-N-Trimethyllysine hydroxylase (EC ) is the first enzyme in the biosynthetic pathway of l-carnitine and catalyzes the formation of beta-hydroxy-N-epsilon-trimethyllysine from epsilon-N-trimethyllysine, a reaction dependent on alpha-ketoglutarate, Fe(2+), and oxygen. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | Citric acid cycle, Carnitine biosynthesis |
+ |
SDH | down-regulates quantity
chemical modification
|
succinate(2-) |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-266276 |
|
|
Homo sapiens |
|
pmid |
sentence |
16143825 |
Mitochondrial succinate dehydrogenase (SDH) consists merely of four nuclearly encoded subunits. It participates in the electron transfer in the respiratory chain and in succinate catabolism in the Krebs cycle. The SDH enzyme, also known as respiratory chain complex II, faces the mitochondrial matrix and is bound to the inner membrane. The human enzyme readily oxidizes succinate to fumarate, while the reverse reaction is hardly detectable in most human cells and tissues under standard conditions. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | Citric acid cycle |
+ |
TMLHE | up-regulates quantity
chemical modification
|
succinate(2-) |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-269683 |
|
|
Homo sapiens |
|
pmid |
sentence |
11431483 |
Epsilon-N-Trimethyllysine hydroxylase (EC ) is the first enzyme in the biosynthetic pathway of l-carnitine and catalyzes the formation of beta-hydroxy-N-epsilon-trimethyllysine from epsilon-N-trimethyllysine, a reaction dependent on alpha-ketoglutarate, Fe(2+), and oxygen. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | Carnitine biosynthesis |
+ |
Succinyl-CoA ATP variant | up-regulates quantity
chemical modification
|
succinate(2-) |
0.8 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-266269 |
|
|
Homo sapiens |
|
pmid |
sentence |
27487822 |
In the citric acid cycle, succinyl-CoA synthetase (SCS) catalyzes the only step that provides substrate-level phosphorylation: succinyl-CoA + NDP + Pi = succinate + CoA + NTP, where N is adenosine or guanosine and the reaction requires magnesium ions. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Pathways: | Citric acid cycle |