| + |
ACADS | up-regulates quantity
chemical modification
|
trans-hex-2-enoyl-CoA(4-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280396 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21237683 |
Long-chain fatty acids are an important source of energy in muscle and heart where the acyl-CoA dehydrogenases (ACADs) participate in consecutive cycles of β-oxidation to generate acetyl-CoA and reducing equivalents for generating energy. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
hexanoyl-CoA(4-) | up-regulates quantity
precursor of
|
trans-hex-2-enoyl-CoA(4-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280398 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 21237683 |
Long-chain fatty acids are an important source of energy in muscle and heart where the acyl-CoA dehydrogenases (ACADs) participate in consecutive cycles of β-oxidation to generate acetyl-CoA and reducing equivalents for generating energy. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ECHS1 | down-regulates quantity
chemical modification
|
trans-hex-2-enoyl-CoA(4-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280400 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 40804397 |
The ECHS1 (short-chain enoyl-CoA hydratase 1) gene is critical for mitochondrial fatty acid β-oxidation and branched-chain amino acid metabolism. In particular, enzymatic assays and molecular characterization from the late 20th to early 21st century confirmed that ECHS1 catalyzes the hydration of short-chain enoyl-CoA, a key step in mitochondrial β-oxidation, essential for metabolic stability. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
trans-hex-2-enoyl-CoA(4-) | up-regulates quantity
precursor of
|
(S)-3-hydroxyhexanoyl-CoA |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280402 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 40804397 |
The ECHS1 (short-chain enoyl-CoA hydratase 1) gene is critical for mitochondrial fatty acid β-oxidation and branched-chain amino acid metabolism. In particular, enzymatic assays and molecular characterization from the late 20th to early 21st century confirmed that ECHS1 catalyzes the hydration of short-chain enoyl-CoA, a key step in mitochondrial β-oxidation, essential for metabolic stability. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |