| + |
very long-chain (R)-3-hydroxyacyl-CoA(4-) | up-regulates quantity 
precursor of
|
very long-chain 2,3-trans-enoyl CoA(4-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267916 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18554507 |
Very long-chain fatty acids are produced through a four-step cycle. Mammals have four candidates, HACD1-4, based on sequence similarities to the recently identified yeast Phs1, although HACD3 and HACD4 share relatively weak similarity. We demonstrate that all four of these human proteins are indeed 3-hydroxyacyl-CoA dehydratases.We also established that the HACD proteins interact with ELOVL proteins. Our analyses have completed the identification of mammalian enzymes responsible for the entire VLCFA elongation cycle. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Fatty Acid Synthesis |
| + |
HACD | down-regulates quantity 
chemical modification
|
very long-chain (R)-3-hydroxyacyl-CoA(4-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-267917 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 18554507 |
Very long-chain fatty acids are produced through a four-step cycle. Mammals have four candidates, HACD1-4, based on sequence similarities to the recently identified yeast Phs1, although HACD3 and HACD4 share relatively weak similarity. We demonstrate that all four of these human proteins are indeed 3-hydroxyacyl-CoA dehydratases.We also established that the HACD proteins interact with ELOVL proteins. Our analyses have completed the identification of mammalian enzymes responsible for the entire VLCFA elongation cycle. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Fatty Acid Synthesis |
3.0
very long-chain (R)-3-hydroxyacyl-CoA(4-)