Structure, mechanism and regulation of pyruvate carboxylase.

@article{Jitrapakdee2008StructureMA,
  title={Structure, mechanism and regulation of pyruvate carboxylase.},
  author={Sarawut Jitrapakdee and Martin St. Maurice and Ivan Rayment and W. Wallace Cleland and J. C. Wallace and Paul V. Attwood},
  journal={The Biochemical journal},
  year={2008},
  volume={413 3},
  pages={369-87}
}
PC (pyruvate carboxylase) is a biotin-containing enzyme that catalyses the HCO(3)(-)- and MgATP-dependent carboxylation of pyruvate to form oxaloacetate. This is a very important anaplerotic reaction, replenishing oxaloacetate withdrawn from the tricarboxylic acid cycle for various pivotal biochemical pathways. PC is therefore considered as an enzyme that is crucial for intermediary metabolism, controlling fuel partitioning toward gluconeogenesis or lipogenesis and in insulin secretion. The… CONTINUE READING
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Distribution and biological functions of pyruvate carboxylase in nature, In Pyruvate Carboxylase (Keech

  • J. Wallace
  • 1985
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