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Alpha-Keto Acid Dehydrogenase Complexes

  • Book
  • © 1996

Overview

Editors:
  1. Mulchand S. Patel

    1. Department of Biochemistry School of Medicine and Biomedical Sciences, State University of New York, Buffalo, USA

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  2. Thomas E. Roche

    1. Department of Biochemistry, Kansas State University, Manhattan, USA

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    You can also search for this editor in PubMed   Google Scholar

  3. Robert A. Harris

    1. Department of Biochemistry and Molecular Biology, Indiana University School of Medicine, Indianapolis, USA

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    You can also search for this editor in PubMed   Google Scholar

Part of the book series: Molecular and Cell Biology Updates (MCBU)

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Table of contents (21 chapters)

  1. Front Matter

    Pages I-IX
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  2. Interaction of protein domains in the assembly and mechanism of 2-oxo acid dehydrogenase multienzyme complexes

    • R. N. Perham
    Pages 1-15

  3. Probing the active site of mammalian pyruvate dehydrogenase

    • L. G. Korotchkina, M. S. Ali, M. S. Patel
    Pages 17-32

  4. Role of the E2 core in the dominant mechanisms of regulatory control of mammalian pyruvate dehydrogenase complex

    • T. E. Roche, S. Liu, S. Ravindran, J. C. Baker, L. Wang
    Pages 33-52

  5. Lipoamide dehydrogenase

    • A. de Kok, W. J. H. van Berkel
    Pages 53-70

  6. Plant pyruvate dehydrogenase complexes

    • M. H. Luethy, J. A. Miernyk, N. R. David, D. D. Randall
    Pages 71-92

  7. Regulation of the pyruvate dehydrogenase complex during the aerobic/anaerobic transition in the development of the parasitic nematode, Ascaris suum

    • R. Komuniecki, M. Klingbeil, R. Arnette, D. Walker, F. Diaz
    Pages 93-99

  8. Structure, function and assembly of mammalian branched-chain α-ketoacid dehydrogenase complex

    • R. M. Wynn, J. R. Davie, M. Meng, D. T. Chuang
    Pages 101-117

  9. Lipoylation of E2 component

    • Y. Motokawa, K. Fujiwara, K. Okamura-Ikeda
    Pages 119-130

  10. Pyruvate dehydrogenase phosphatase

    • L. J. Reed, J. E. Lawson, X.-D. Niu, J. Yan
    Pages 131-138

  11. The mitochondrial α-ketoacid dehydrogenase kinases: Molecular cloning, tissue-specific expression and primary structure analysis

    • R. A. Harris, K. M. Popov
    Pages 139-149

  12. Shorter term and longer term regulation of pyruvate dehydrogenase kinases

    • P. J. Randle, D. A. Priestman
    Pages 151-161

  13. Hormonal and nutritional modulation of PDHC activity status

    • M. C. Sugden, M. J. Holness
    Pages 163-176

  14. Regulation of branched-chain α-keto acid dehydrogenase complex in rat liver and skeletal muscle by exercise and nutrition

    • Y. Shimomura
    Pages 177-186

  15. Dephosphorylation of PDH by phosphoprotein phosphatases and its allosteric regulation by inositol glycans

    • S. Abe, L. C. Huang, J. Larner
    Pages 187-195

  16. Long-term regulation and promoter analysis of mammalian pyruvate dehydrogenase complex

    • M. S. Patel, S. Naik, M. Johnson, R. Dey
    Pages 197-211

  17. The sperm-specific pyruvate dehydrogenase E1α genes

    • H.-H. M. Dahl, J. Fitzgerald, R. Iannello
    Pages 213-226

  18. Molecular defects of the branched-chain α-keto acid dehydrogenase complex: Maple syrup urine disease due to mutations of the E1α or E1β subunit gene

    • Y. Indo, I. Matsuda
    Pages 227-247

  19. Human defects of the pyruvate dehydrogenase complex

    • D. S. Kerr, I. D. Wexler, A. Tripatara, M. S. Patel
    Pages 249-269

  20. Multigenic basis for maple syrup urine disease with emphasis on mutations in branched chain dihydrolipoyl acyltransferase

    • D. J. Danner, M. C. McKean
    Pages 271-293
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Keywords

About this book

Found in all organisms, the alpha-keto acid dehydrogenase complexes have central roles in cellular metabolism and are major sites of regulation. The understanding of the organization, function and regulation of these quintessential multienzyme complexes has been greatly advanced by studies employing molecular biology and biophysical techniques. Although these enzyme systems have some features in common, their diversity in fulfilling unique organism - or tissue - specific roles is truly amazing. These systems have medical importance in areas ranging from defects in regulation (linked to diabetes, heart disease, obesity, nutrition defects), to inherited diseases (inborn errors, maple syrup urine disease) to acquired immune diseases (primary biliary cirrhosis). This book brings together wide-ranging recent findings on the structure(function relationships, gene regulation, and genetic defects of the alpha-keto acid dehydrogenase complexes, namely the pyruvate dehydrogenase, alpha-ketoglutarate dehydrogenase and the branched-chain alpha-keto acid dehydrogenase complexes. A wide variety of experimental approaches together with new results presented in this book should serve as a resource for beginning to established investigators in the field as well as scientists who are interested in mitochondria, dehydrogenases, kinases, phosphatases, lipoic acid, thiamine pyrophosphate, and enzyme complexes.

Editors and Affiliations

  • Department of Biochemistry School of Medicine and Biomedical Sciences, State University of New York, Buffalo, USA

    Mulchand S. Patel

  • Department of Biochemistry, Kansas State University, Manhattan, USA

    Thomas E. Roche

  • Department of Biochemistry and Molecular Biology, Indiana University School of Medicine, Indianapolis, USA

    Robert A. Harris

Bibliographic Information

  • Book Title: Alpha-Keto Acid Dehydrogenase Complexes

  • Editors: Mulchand S. Patel, Thomas E. Roche, Robert A. Harris

  • Series Title: Molecular and Cell Biology Updates

  • DOI: https://doi.org/10.1007/978-3-0348-8981-0

  • Publisher: Birkhäuser Basel

  • eBook Packages: Springer Book Archive

  • Copyright Information: Birkhäuser Verlag 1996

  • Softcover ISBN: 978-3-0348-9853-9Published: 30 September 2011

  • eBook ISBN: 978-3-0348-8981-0Published: 06 December 2012

  • Edition Number: 1

  • Number of Pages: 321

  • Topics: Biochemistry, general, Cell Biology

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