(acetyl-CoA carboxylase) kinase
| [acetyl-CoA carboxylase] kinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.7.11.27 | ||||||||
| CAS no. | 77000-06-7 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
In enzymology, a [acetyl-CoA carboxylase] kinase (EC 2.7.11.27) is an enzyme that catalyzes the chemical reaction
- ATP + [acetyl-CoA carboxylase] ADP + [acetyl-CoA carboxylase] phosphate
Thus, the two substrates of this enzyme are ATP and acetyl-CoA carboxylase, whereas its two products are ADP and acetyl-CoA carboxylase phosphate.
This enzyme belongs to the family of transferases, specifically those transferring a phosphate group to the sidechain oxygen atom of serine or threonine residues in proteins (protein-serine/threonine kinases). The systematic name of this enzyme class is ATP:[acetyl-CoA carboxylase] phosphotransferase. Other names in common use include acetyl coenzyme A carboxylase kinase (phosphorylating), acetyl-CoA carboxylase bound kinase, acetyl-CoA carboxylase kinase, acetyl-CoA carboxylase kinase (cAMP-independent), acetyl-CoA carboxylase kinase 2, acetyl-CoA carboxylase kinase-2, acetyl-CoA carboxylase kinase-3 (AMP-activated), acetyl-coenzyme A carboxylase kinase, ACK2, ACK3, AMPK, I-peptide kinase, and STK5.
References
- Jamil H, Madsen NB (1987). "Phosphorylation state of acetyl-coenzyme A carboxylase. I. Linear inverse relationship to activity ratios at different citrate concentrations". J. Biol. Chem. 262 (2): 630–7. PMID 2879833.
- Lent B, Kim KH (1982). "Purification and properties of a kinase which phosphorylates and inactivates acetyl-CoA carboxylase". J. Biol. Chem. 257 (4): 1897–901. PMID 6120170.
- Munday MR, Hardie DG (1984). "Isolation of three cyclic-AMP-independent acetyl-CoA carboxylase kinases from lactating rat mammary gland and characterization of their effects on enzyme activity". Eur. J. Biochem. 141 (3): 617–27. doi:10.1111/j.1432-1033.1984.tb08237.x. PMID 6146523.
- Mohamed AH, Huang WY, Huang W, Venkatachalam KV, Wakil SJ (1994). "Isolation and characterization of a novel acetyl-CoA carboxylase kinase from rat liver". J. Biol. Chem. 269 (9): 6859–65. PMID 7907095.
- Heesom KJ, Moule SK, Denton RM (1998). "Purification and characterisation of an insulin-stimulated protein-serine kinase which phosphorylates acetyl-CoA carboxylase". FEBS Lett. 422 (1): 43–6. doi:10.1016/S0014-5793(97)01597-4. PMID 9475166.
