| + |
Cytochrome c oxidase-Mitochondrial respiratory chain complex IV | up-regulates quantity 
chemical modification
|
water |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280295 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10563795 |
Cytochrome c oxidase catalyzes the reduction of molecular oxygen to water, a process in which four electrons, four protons, and one molecule of oxygen are consumed. The reaction is coupled to the pumping of four additional protons across the membrane. According to the currently accepted concept, the pumping of all four protons occurs after the binding of oxygen to the reduced enzyme and is exclusively coupled to the last two electron transfer steps. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AMPD2 | down-regulates quantity 
chemical modification
|
water |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280486 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 26321268 |
AMP deaminase (AMPD; EC 3.5.4.6) catalyzes hydrolysis of the amino group from the adenine ring of AMP resulting in production of inosine 5'-monophosphate (IMP) and ammonia. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
AMPD3 | down-regulates quantity
chemical modification
|
water |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280491 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 26321268 |
AMP deaminase (AMPD; EC 3.5.4.6) catalyzes hydrolysis of the amino group from the adenine ring of AMP resulting in production of inosine 5'-monophosphate (IMP) and ammonia. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ECHS1 | down-regulates quantity
chemical modification
|
water |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280367 |
|
|
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. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280345 |
|
|
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. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280420 |
|
|
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: |
3 |
Organism: |
Homo Sapiens |
| + |
Trifunctional enzyme | down-regulates quantity
chemical modification
|
water |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280313 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 30850536 |
Membrane-bound mitochondrial trifunctional protein (TFP) catalyzes β-oxidation of long chain fatty acyl-CoAs, employing 2-enoyl-CoA hydratase (ECH), 3- hydroxyl-CoA dehydrogenase (HAD), and 3-ketothiolase (KT) activities consecutively. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280332 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 29551309 |
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. 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. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
AMPD1 | down-regulates quantity
chemical modification
|
water |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280481 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 26321268 |
AMP deaminase (AMPD; EC 3.5.4.6) catalyzes hydrolysis of the amino group from the adenine ring of AMP resulting in production of inosine 5'-monophosphate (IMP) and ammonia. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MAPDA | down-regulates quantity
chemical modification
|
water |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280496 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 29884623 |
We show that Arabidopsis thaliana and human cells require an N6-mAMP deaminase (ADAL, renamed MAPDA) to catabolize N6-mAMP to inosine monophosphate in vivo by hydrolytically removing the aminomethyl group. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280502 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 29884623 |
We show that Arabidopsis thaliana and human cells require an N6-mAMP deaminase (ADAL, renamed MAPDA) to catabolize N6-mAMP to inosine monophosphate in vivo by hydrolytically removing the aminomethyl group. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
4.0
water