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Structure and function of a single-chain, multi-domain long-chain acyl-CoA carboxylase

Author

Listed:
  • Timothy H. Tran

    (Columbia University)

  • Yu-Shan Hsiao

    (Harvard Medical School
    Present addresses: Department of Otolaryngology, Massachusetts Eye and Ear Infirmary, Boston, Massachusetts 02114, USA (Y.-S.H.); Department of Life Sciences and Institute of Genome Sciences, National Yang-Ming University, Taipei 112, Taiwan (C.-Y.C.).)

  • Jeanyoung Jo

    (Columbia University)

  • Chi-Yuan Chou

    (Columbia University
    Present addresses: Department of Otolaryngology, Massachusetts Eye and Ear Infirmary, Boston, Massachusetts 02114, USA (Y.-S.H.); Department of Life Sciences and Institute of Genome Sciences, National Yang-Ming University, Taipei 112, Taiwan (C.-Y.C.).)

  • Lars E. P. Dietrich

    (Columbia University)

  • Thomas Walz

    (Harvard Medical School
    Howard Hughes Medical Institute, Harvard Medical School)

  • Liang Tong

    (Columbia University)

Abstract

A novel biotin-dependent carboxylase with a preference for long-chain acyl-CoA substrates and a unique holoenzyme architecture is described.

Suggested Citation

  • Timothy H. Tran & Yu-Shan Hsiao & Jeanyoung Jo & Chi-Yuan Chou & Lars E. P. Dietrich & Thomas Walz & Liang Tong, 2015. "Structure and function of a single-chain, multi-domain long-chain acyl-CoA carboxylase," Nature, Nature, vol. 518(7537), pages 120-124, February.
    • Handle: RePEc:nat:nature:v:518:y:2015:i:7537:d:10.1038_nature13912
    DOI: 10.1038/nature13912
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