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Role of reversible phosphorylation of acetyl‐CoA carboxylase in long‐chain fatty acid synthesis 1
Author(s) -
Kim KiHan,
LópezCasillas F.,
Bai D. H.,
Luo X.,
Pape M. E.
Publication year - 1989
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.3.11.2570725
Subject(s) - acetyl coa carboxylase , phosphorylation , dephosphorylation , pyruvate carboxylase , biochemistry , fatty acid synthesis , lipogenesis , atp citrate lyase , chemistry , kinase , enzyme , citrate synthase , phosphatase , lipid metabolism
Acetyl‐CoA carboxylase, the rate‐limiting enzyme in the biogenesis of long‐chain fatty acids, is regulated by phosphorylation and dephosphorylation. The major phosphorylation sites that affect carboxylase activity and the specific protein kinases responsible for phosphorylation of different sites have been identified. A form of acetyl‐CoA carboxylase that is independent of citrate for activity occurs in vivo. This active form of caboxylase becomes citrate‐dependent upon phosphorylation under conditions of reduced lipogenesis. Therefore, phosphorylation‐dephosphorylation of acetyl‐CoA carboxylase is the enzyme's primary short‐term regulatory mechanism; this control mechanism together with cellular metabolites such as CoA, citrate, and palmitoyl‐CoA serves to fine‐tune the synthesis of long‐chain fatty acids under different physiological conditions.— K im , K.‐H.; L ópez ‐C asillas , F.; B ai , D. H.; L uo , X.; P ape , M. E. Physiological significance of covalent phosphorylation‐dephosphorylation of acetyl‐CoA carboxylase in the regulation of long‐chain fatty acids. FASEB J. 3: 2250‐2256; 1989.