The Enzyme Database

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Accepted name: [acetyl-CoA carboxylase] kinase
Reaction: ATP + [acetyl-CoA carboxylase] = ADP + [acetyl-CoA carboxylase] phosphate
Other name(s): 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; STK5
Systematic name: ATP:[acetyl-CoA carboxylase] phosphotransferase
Comments: Phosphorylates and inactivates EC, acetyl-CoA carboxylase, which can be dephosphorylated and reactivated by EC, [phosphorylase] phosphatase. The enzyme is more active towards the dimeric form of acetyl-CoA carboxylase than the polymeric form [5]. Phosphorylates serine residues.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 77000-06-7
1.  Jamil, H. and Madsen, N.B. Phosphorylation state of acetyl-coenzyme A carboxylase. I. Linear inverse relationship to activity ratios at different citrate concentrations. J. Biol. Chem. 262 (1987) 630–637. [PMID: 2879833]
2.  Lent, B. and Kim, K.H. Purification and properties of a kinase which phosphorylates and inactivates acetyl-CoA carboxylase. J. Biol. Chem. 257 (1982) 1897–1901. [PMID: 6120170]
3.  Munday, M.R. and Hardie, D.G. 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 (1984) 617–627. [PMID: 6146523]
4.  Mohamed, A.H., Huang, W.Y., Huang, W., Venkatachalam, K.V. and Wakil, S.J. Isolation and characterization of a novel acetyl-CoA carboxylase kinase from rat liver. J. Biol. Chem. 269 (1994) 6859–6865. [PMID: 7907095]
5.  Heesom, K.J., Moule, S.K. and Denton, R.M. Purification and characterisation of an insulin-stimulated protein-serine kinase which phosphorylates acetyl-CoA carboxylase. FEBS Lett. 422 (1998) 43–46. [PMID: 9475166]
[EC created 1990 as EC (EC created 1984, incorporated 1992), transferred 2005 to EC]

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