Structure-function analysis of enoyl thioester reductase involved in mitochondrial maintenance.

@article{Airenne2003StructurefunctionAO,
  title={Structure-function analysis of enoyl thioester reductase involved in mitochondrial maintenance.},
  author={Tomi T Airenne and Juha M Torkko and Sam Van den plas and Raija T. Sormunen and Alexander J Kastaniotis and Rik Wierenga and J Kalervo Hiltunen},
  journal={Journal of molecular biology},
  year={2003},
  volume={327 1},
  pages={47-59}
}
Candida tropicalis enoyl thioester reductase Etr1p and the Saccharomyces cerevisiae homologue Mrf1p catalyse the NADPH-dependent reduction of trans-2-enoyl thioesters in mitochondrial fatty acid synthesis (FAS). Unlike prokaryotic enoyl thioester reductases (ETRs), which belong to the short-chain dehydrogenases/reductases (SDR), Etr1p and Mrf1p represent structurally distinguishable ETRs that belong to the medium-chain dehydrogenases/reductases (MDR) superfamily, indicating independent origin… CONTINUE READING

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