EC Number   |
Natural Substrates |
|---|
   2.7.11.27 | ATP + [acetyl-CoA carboxylase] |
- |
| 2.7.11.27 | ATP + [acetyl-CoA carboxylase] |
involved in insulin dependent regulation of acetyl-CoA carboxylase in vivo |
| 2.7.11.27 | ATP + [acetyl-CoA carboxylase] |
phosphorylates and inactivates acetyl-CoA carboxylase, (EC 6.4.1.2), and is therefore involved in regulation of long chain fatty acid synthesis |
| 2.7.11.27 | ATP + [acetyl-CoA carboxylase] |
acetyl-CoA carboxylase bound kinase involved in regulation in vivo |
| 2.7.11.27 | ATP + [acetyl-CoA carboxylase] |
most likely candidate for acetyl-CoA carboxylase inactivation in vivo |
| 2.7.11.27 | ATP + [acetyl-CoA carboxylase] |
ACK3 and not ACK2 appears to be responsible for acetyl-CoA carboxylase inactivation in lactating mammary gland |
| 2.7.11.27 | ATP + [acetyl-CoA carboxylase] |
regulation of acetyl-CoA carboxylase in muscle at metabolic stress conditions |
| 2.7.11.27 | ATP + [acetyl-CoA carboxylase] |
acetyl-CoA carboxylase from skeletal muscle is more potently inhibited by palmitoyl-CoA after having been phosphorylated by AMPK. This may contribute to low muscle malonyl-CoA values and increasing fatty acid oxidation rates during long-term exercise when plasma fatty acid concentrations are elevated |
| 2.7.11.27 | ATP + [acetyl-CoA carboxylase] |
AMPK causes phosphorylation and inhibition of acetyl-CoA carboxylase, which reduces the production of malonyl-CoA |
| 2.7.11.27 | ATP + [acetyl-CoA carboxylase] |
AMPKalpha negatively regulates activity of acetyl-CoA carboxylase and hepatic lipid content |
