| + |
NADH-ubiquinone oxidoreductase-Mitochondrial respiratory chain complex I | down-regulates quantity 
chemical modification
|
NADH(2-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280279 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12231006 |
The energy-transducing NADH: quinone (Q) oxidoreductase (complex I) is the largest and most complicated enzyme complex in the oxidative phosphorylation system. Complex I is a redox pump that uses the redox energy to translocate H(+) (or Na(+)) ions across the membrane, resulting in a significant contribution to energy production. Complex I is located at an entry point of the electron transport chain and initiates electron transfer by oxidizing NADH and the electrons are transferred to a lipid-soluble electron carrier quinone (coenzyme Q) as an electron acceptor. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
NADH(2-) | up-regulates quantity 
precursor of
|
NAD(1-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-280286 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12231006 |
The energy-transducing NADH: quinone (Q) oxidoreductase (complex I) is the largest and most complicated enzyme complex in the oxidative phosphorylation system. Complex I is a redox pump that uses the redox energy to translocate H(+) (or Na(+)) ions across the membrane, resulting in a significant contribution to energy production. Complex I is located at an entry point of the electron transport chain and initiates electron transfer by oxidizing NADH and the electrons are transferred to a lipid-soluble electron carrier quinone (coenzyme Q) as an electron acceptor. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Carnitine biosynthesis |
| + |
ALDH9A1 | up-regulates quantity
chemical modification
|
NADH(2-) |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-269695 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 11802770 |
Aldolytic cleavage of HTML yields 4-trimethylaminobutyraldehyde (TMABA) and glycine, a reaction catalysed by HTML aldolase (HTMLA; EC 4.1.2.‘X’). Dehydrogenation of TMABA by TMABA dehydrogenase (TMABA-DH; EC 1.2.1.47) results in the formation of 4-Ntrimethylaminobutyrate (butyrobetaine). |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Carnitine biosynthesis |
4.0
NADH(2-)