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Interaction of Substrate and Pterin Cofactor with the Metal of Human Tyrosine Hydroxylase as Determined by 1H-NMR

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Chemistry and Biology of Pteridines and Folates

Part of the book series: Advances in Experimental Medicine and Biology ((AEMB,volume 338))

Abstract

Tyrosine hydroxylase (EC 1.14.16.2, TH) catalyses the rate-limiting step in the biosynthesis of catecholamines. Human TH exists as four different isoforms (hTHl to hTH4) which have been expressed in E. coli 1. The purified apoenzymes are rapidly activated (up to 40-fold) by the incorporation of stoichiometric amounts of Fe++ 2. All isozymes are competitively inhibited by other divalent metal ions, e.g. Zn++, Co++ and Ni++ which bind with similar affinity and stoichiometry as Fe++ 2,3.

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Author information

Authors and Affiliations

  1. Department of Biochemistry and Molecular Biology, University of Bergen, N-5009, Bergen, Norway

    Aurora Martínez, Jan Haavik & Torgeir Flatmark

  2. Department of Biological Chemistry, The Johns Hopkins University School of Medicine, Baltimore, Maryland, 21205, USA

    Chitrananda Abeygunawardana & Albert S. Mildvan

Authors
  1. Aurora Martínez
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  2. Chitrananda Abeygunawardana
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  3. Jan Haavik
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  4. Torgeir Flatmark
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  5. Albert S. Mildvan
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Editor information

Editors and Affiliations

  1. Dept of Pharmacology College of Medicine, Universily of South Alabama, Mobile, AL, 36688, USA

    June E. Ayling

  2. Dept. of Biochemistry College of Medicine, University of South Alabama, Mobile, AL, 36688, USA

    M. Gopal Nair

  3. College of Medicine, Universily of South Alabama, Mobile, AL, 36688, USA

    Charles M. Baugh

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© 1993 Springer Science+Business Media New York

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Martínez, A., Abeygunawardana, C., Haavik, J., Flatmark, T., Mildvan, A.S. (1993). Interaction of Substrate and Pterin Cofactor with the Metal of Human Tyrosine Hydroxylase as Determined by 1H-NMR. In: Ayling, J.E., Nair, M.G., Baugh, C.M. (eds) Chemistry and Biology of Pteridines and Folates. Advances in Experimental Medicine and Biology, vol 338. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-2960-6_15

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  • DOI: https://doi.org/10.1007/978-1-4615-2960-6_15

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4613-6287-6

  • Online ISBN: 978-1-4615-2960-6

  • eBook Packages: Springer Book Archive

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