| + |
(S)-3-hydroxybutanoyl-CoA | up-regulates quantity 
precursor of
|
acetoacetyl-CoA(4-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280425 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16176262 |
3-Hydroxyacyl-CoA dehydrogenase (HAD) functions in mitochondrial fatty acid beta-oxidation by catalyzing the oxidation of straight chain 3-hydroxyacyl-CoAs. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ACAT1 | down-regulates quantity 
chemical modification
|
acetoacetyl-CoA(4-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280426 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 31268215 |
The mitochondrial acetoacetyl‐CoA thiolase (commonly known as β‐ketothiolase [T2]; EC 2.3.1.9; encoded by the ACAT1 gene) is a ubiquitous and important enzyme for ketone body synthesis and degradation as well as in isoleucine catabolismIn the biosynthetic direction, thiolases catalyze the formation of a carbon‐carbon bond through a Claisen condensation mechanism (from two acetyl‐CoA molecules) and in the reverse, degradative direction a C‐C bond is broken through thiolysis (in the presence of CoA), resulting in chain shortening of the acyl chain by two carbon atoms (in case the substrate is an unbranched acyl chain) or by three atoms (in case the substrate is a 2‐methyl‐branched acyl chain), such as for example catalyzed by the T2 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ACAT1 | up-regulates quantity
precursor of
|
acetoacetyl-CoA(4-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280431 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 31268215 |
The mitochondrial acetoacetyl‐CoA thiolase (commonly known as β‐ketothiolase [T2]; EC 2.3.1.9; encoded by the ACAT1 gene) is a ubiquitous and important enzyme for ketone body synthesis and degradation as well as in isoleucine catabolismIn the biosynthetic direction, thiolases catalyze the formation of a carbon‐carbon bond through a Claisen condensation mechanism (from two acetyl‐CoA molecules) and in the reverse, degradative direction a C‐C bond is broken through thiolysis (in the presence of CoA), resulting in chain shortening of the acyl chain by two carbon atoms (in case the substrate is an unbranched acyl chain) or by three atoms (in case the substrate is a 2‐methyl‐branched acyl chain), such as for example catalyzed by the T2 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
HMGCS2 | down-regulates quantity
chemical modification
|
acetoacetyl-CoA(4-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-282483 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11479731 |
Mitochondrial 3-hydroxy-3-methylglutaryl-CoA synthase (mHMGS: EC 4.1.3.5) catalyses the first step of ketogenesis from acetyl-CoA and acetoacetyl-CoA and is considered to be the main control step in ketogenesis (Hegardt 1999). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
acetoacetyl-CoA(4-) | up-regulates quantity
precursor of
|
(3S)-3-hydroxy-3-methylglutaryl-CoA |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-282487 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11479731 |
Mitochondrial 3-hydroxy-3-methylglutaryl-CoA synthase (mHMGS: EC 4.1.3.5) catalyses the first step of ketogenesis from acetyl-CoA and acetoacetyl-CoA and is considered to be the main control step in ketogenesis (Hegardt 1999). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
OXCT1 | up-regulates quantity
chemical modification
|
acetoacetyl-CoA(4-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-282507 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10964512 |
Succinyl-CoA:3-ketoacid-CoA transferase (SCOT2 ; EC 2.8.3.5), a mitochondrial homodimer essential for ketone body utilization, catalyzes the activation of acetoacetate to acetoacetyl-CoA. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
acetoacetic acid | up-regulates quantity
precursor of
|
acetoacetyl-CoA(4-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-282509 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10964512 |
Succinyl-CoA:3-ketoacid-CoA transferase (SCOT2 ; EC 2.8.3.5), a mitochondrial homodimer essential for ketone body utilization, catalyzes the activation of acetoacetate to acetoacetyl-CoA. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
OXCT2 | up-regulates quantity
chemical modification
|
acetoacetyl-CoA(4-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-282513 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10964512 |
Succinyl-CoA:3-ketoacid-CoA transferase (SCOT2 ; EC 2.8.3.5), a mitochondrial homodimer essential for ketone body utilization, catalyzes the activation of acetoacetate to acetoacetyl-CoA. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AACS | up-regulates quantity
chemical modification
|
acetoacetyl-CoA(4-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-282525 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 37356666 |
Acetoacetyl-CoA synthetase (AACS) is the key enzyme in the anabolic utilization of ketone bodies (KBs) for denovo lipid synthesis, a process that bypasses citrate and ATP citrate lyase. Acetoacetyl-CoA (AcAc-CoA) synthetase (AACS) (AcAc-CoA ligase, Enzyme Commission no.: 6.2.1.16) is a cytosolic lipogenic enzyme found in many tissues involved in lipid synthesis (1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11). It catalyzes the coupling of acetoacetate (AcAc), one of the ketone bodies (KBs), to CoA in the reaction shown below to produce cytosolic AcAc-CoA. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
coenzyme A(4-) | up-regulates quantity
precursor of
|
acetoacetyl-CoA(4-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-282526 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 37356666 |
Acetoacetyl-CoA synthetase (AACS) is the key enzyme in the anabolic utilization of ketone bodies (KBs) for denovo lipid synthesis, a process that bypasses citrate and ATP citrate lyase. Acetoacetyl-CoA (AcAc-CoA) synthetase (AACS) (AcAc-CoA ligase, Enzyme Commission no.: 6.2.1.16) is a cytosolic lipogenic enzyme found in many tissues involved in lipid synthesis (1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11). It catalyzes the coupling of acetoacetate (AcAc), one of the ketone bodies (KBs), to CoA in the reaction shown below to produce cytosolic AcAc-CoA. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
acetoacetate | up-regulates quantity
precursor of
|
acetoacetyl-CoA(4-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-282527 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 37356666 |
Acetoacetyl-CoA synthetase (AACS) is the key enzyme in the anabolic utilization of ketone bodies (KBs) for denovo lipid synthesis, a process that bypasses citrate and ATP citrate lyase. Acetoacetyl-CoA (AcAc-CoA) synthetase (AACS) (AcAc-CoA ligase, Enzyme Commission no.: 6.2.1.16) is a cytosolic lipogenic enzyme found in many tissues involved in lipid synthesis (1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11). It catalyzes the coupling of acetoacetate (AcAc), one of the ketone bodies (KBs), to CoA in the reaction shown below to produce cytosolic AcAc-CoA. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
HADH | up-regulates quantity
chemical modification
|
acetoacetyl-CoA(4-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280424 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 16176262 |
3-Hydroxyacyl-CoA dehydrogenase (HAD) functions in mitochondrial fatty acid beta-oxidation by catalyzing the oxidation of straight chain 3-hydroxyacyl-CoAs. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
acetoacetyl-CoA(4-) | up-regulates quantity
precursor of
|
acetyl-CoA(4-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280428 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 31268215 |
The mitochondrial acetoacetyl‐CoA thiolase (commonly known as β‐ketothiolase [T2]; EC 2.3.1.9; encoded by the ACAT1 gene) is a ubiquitous and important enzyme for ketone body synthesis and degradation as well as in isoleucine catabolismIn the biosynthetic direction, thiolases catalyze the formation of a carbon‐carbon bond through a Claisen condensation mechanism (from two acetyl‐CoA molecules) and in the reverse, degradative direction a C‐C bond is broken through thiolysis (in the presence of CoA), resulting in chain shortening of the acyl chain by two carbon atoms (in case the substrate is an unbranched acyl chain) or by three atoms (in case the substrate is a 2‐methyl‐branched acyl chain), such as for example catalyzed by the T2 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
4.0
acetoacetyl-CoA(4-)