| + |
Trifunctional enzyme | up-regulates quantity 
chemical modification
|
lauroyl-CoA(4-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280339 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 29551309 |
The second step in the β-oxidation of fatty acids is the hydration of the trans-double bond to generate a 3-l-hydroxyacyl-coA ester, catalyzed by enoyl-coA hydratase. In the third step, 3-l-hydroxyacyl-coA dehydrogenase catalyzes the oxidation of the 3-l-hydroxyacyl-coA ester to a 3-ketoacyl-coA intermediate while NADH is generated from NAD+. The fourth and final step is the thiolytic cleavage of the chain by a ketothiolase, generating acetyl-coA and a fatty-acyl-coA two carbon atoms shorter. This shortened acyl-coA ester may start again the oxidation cycle. (Fig. 3) In humans, a single enzyme catalyzes the three last steps in the β-oxidation of long-chain fatty acids, the mitochondrial trifunctional protein (MTP) complex |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
3-oxotetradecanoyl-CoA | up-regulates quantity
precursor of
|
lauroyl-CoA(4-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280340 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 29551309 |
The second step in the β-oxidation of fatty acids is the hydration of the trans-double bond to generate a 3-l-hydroxyacyl-coA ester, catalyzed by enoyl-coA hydratase. In the third step, 3-l-hydroxyacyl-coA dehydrogenase catalyzes the oxidation of the 3-l-hydroxyacyl-coA ester to a 3-ketoacyl-coA intermediate while NADH is generated from NAD+. The fourth and final step is the thiolytic cleavage of the chain by a ketothiolase, generating acetyl-coA and a fatty-acyl-coA two carbon atoms shorter. This shortened acyl-coA ester may start again the oxidation cycle. (Fig. 3) In humans, a single enzyme catalyzes the three last steps in the β-oxidation of long-chain fatty acids, the mitochondrial trifunctional protein (MTP) complex |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ACADL | down-regulates quantity 
chemical modification
|
lauroyl-CoA(4-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280341 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18227065 |
Very-long-chain acyl-CoA dehydrogenase (VLCAD) is a member of the family of acyl-CoA dehydrogenases (ACADs). Very-long-chain acyl-CoA dehydrogenase (VLCAD)3 is one of five acyl-CoA dehydrogenases (ACADs) that catalyze the initial, rate-limiting step of mitochondrial fatty acid β-oxidation, with distinct but overlapping fatty acyl chain-length specificities.When myristoyl-CoA was added, the yellow enzyme solution turned colorless, indicating that the enzyme flavin was reduced by the substrate. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
lauroyl-CoA(4-) | up-regulates quantity
precursor of
|
trans-dodec-2-enoyl-CoA(4-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280343 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18227065 |
Very-long-chain acyl-CoA dehydrogenase (VLCAD) is a member of the family of acyl-CoA dehydrogenases (ACADs). Very-long-chain acyl-CoA dehydrogenase (VLCAD)3 is one of five acyl-CoA dehydrogenases (ACADs) that catalyze the initial, rate-limiting step of mitochondrial fatty acid β-oxidation, with distinct but overlapping fatty acyl chain-length specificities.When myristoyl-CoA was added, the yellow enzyme solution turned colorless, indicating that the enzyme flavin was reduced by the substrate. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
4.0
lauroyl-CoA(4-)