Crystal structures and mutational analyses of acyl-CoA carboxylase beta subunit of Streptomyces coelicolor.

@article{Arabolaza2010CrystalSA,
  title={Crystal structures and mutational analyses of acyl-CoA carboxylase beta subunit of Streptomyces coelicolor.},
  author={Ana Arabolaza and Mary Elizabeth Shillito and Ting-Wan Lin and Lautaro Diacovich and M. M. Melgar and Huy Pham and Deborah L Amick and Hugo Gramajo and Shiou-Chuan Tsai},
  journal={Biochemistry},
  year={2010},
  volume={49 34},
  pages={
          7367-76
        }
}
The first committed step of fatty acid and polyketides biosynthesis, the biotin-dependent carboxylation of an acyl-CoA, is catalyzed by acyl-CoA carboxylases (ACCases) such as acetyl-CoA carboxylase (ACC) and propionyl-CoA carboxylase (PCC). ACC and PCC in Streptomyces coelicolor are homologue multisubunit complexes that can carboxylate different short chain acyl-CoAs. While ACC is able to carboxylate acetyl-, propionyl-, or butyryl-CoA with approximately the same specificity, PCC only… 
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