scholarly journals Erratum: A unified molecular mechanism for the regulation of acetyl-CoA carboxylase by phosphorylation

2017 ◽  
Vol 3 (1) ◽  
Author(s):  
Jia Wei ◽  
Yixiao Zhang ◽  
Tai-Yuan Yu ◽  
Kianoush Sadre-Bazzaz ◽  
Michael J Rudolph ◽  
...  
Keyword(s):  
Molecular Mechanism ◽  
Acetyl Coa Carboxylase ◽  
Acetyl Coa

scholarly journals A unified molecular mechanism for the regulation of acetyl-CoA carboxylase by phosphorylation

2016 ◽  
Vol 2 (1) ◽  
Author(s):  
Jia Wei ◽  
Yixiao Zhang ◽  
Tai-Yuan Yu ◽  
Kianoush Sadre-Bazzaz ◽  
Michael J Rudolph ◽  
...  
Keyword(s):  
Drug Discovery ◽  
Molecular Mechanism ◽  
Conformational Changes ◽  
Potent Inhibitor ◽  
Acetyl Coa Carboxylase ◽  
Single Chain ◽  
Electron Microscopic ◽  
Acetyl Coa ◽  
Microscopic Studies ◽  
And Function

Abstract Acetyl-CoA carboxylases (ACCs) are crucial metabolic enzymes and attractive targets for drug discovery. Eukaryotic acetyl-CoA carboxylases are 250 kDa single-chain, multi-domain enzymes and function as dimers and higher oligomers. Their catalytic activity is tightly regulated by phosphorylation and other means. Here we show that yeast ACC is directly phosphorylated by the protein kinase SNF1 at residue Ser1157, which potently inhibits the enzyme. Crystal structure of three ACC central domains (AC3–AC5) shows that the phosphorylated Ser1157 is recognized by Arg1173, Arg1260, Tyr1113 and Ser1159. The R1173A/R1260A double mutant is insensitive to SNF1, confirming that this binding site is crucial for regulation. Electron microscopic studies reveal dramatic conformational changes in the holoenzyme upon phosphorylation, likely owing to the dissociation of the biotin carboxylase domain dimer. The observations support a unified molecular mechanism for the regulation of ACC by phosphorylation as well as by the natural product soraphen A, a potent inhibitor of eukaryotic ACC. These molecular insights enhance our understanding of acetyl-CoA carboxylase regulation and provide a basis for drug discovery.

The role of rice bran extract on acetyl CoA carboxylase in liver of rats fed a high-fat diet

Planta Medica ◽  
2011 ◽  
Vol 77 (12) ◽  
Author(s):  
C Charkhonpunya ◽  
S Sireeratawong ◽  
S Komindr ◽  
N Lerdvuthisopon
Keyword(s):  
Rice Bran ◽  
High Fat Diet ◽  
Acetyl Coa Carboxylase ◽  
High Fat ◽  
Acetyl Coa ◽  
Rice Bran Extract

scholarly journals Polymer-protomer transition of acetyl-CoA carboxylase occurs in vivo and varies with nutritional conditions.

1980 ◽  
Vol 255 (21) ◽  
pp. 10033-10035
Author(s):  
B.A. Ashcraft ◽  
W.S. Fillers ◽  
S.L. Augustine ◽  
S.D. Clarke
Keyword(s):  
Acetyl Coa Carboxylase ◽  
Acetyl Coa ◽  
Nutritional Conditions
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