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Crystallographic Studies of Native and Mutant Orotidine 5′phosphate Decarboxylases

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Orotidine Monophosphate Decarboxylase

Part of the book series: Topics in Current Chemistry ((TOPCURRCHEM,volume 238))

Abstract

This review aims to use the results of an approach combining crystallographic structure analysis with mutational studies as a framework for the various mechanistic proposals advanced in attempts to explain the astonishing acceleration rates displayed by orotidine 5′-monophosphate decarboxylase, the most proficient enzyme known. Special emphasis is placed on the contributions of active site amino acids to the selection and binding of substrate, product, and inhibitors as well as on the identification of alternative binding modes. Finally, a dynamic mechanism is proposed in which an increase in the strength of substrate binding and its catalytic conversion to product progress in parallel.

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Abbreviations

ODCase :

Orotidine 5′-monophosphate decarboxylase

TIM :

Triosephosphate isomerase

r.m.s. :

Root-mean-square

BMP :

6-hydroxyuridine 5′-mono-phosphate

CMP :

Cytidine 5′-monophosphate

OMP :

Orotidine 5′-monophosphate

UMP :

Uridine 5′-monophosphate

XMP :

Xanthine 5′-monophosphate

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Author information

Authors and Affiliations

  1. Department of Biochemistry, University of Toronto, 1 King’s College Circle, Toronto, Ontario, M5S 1A8, Canada

    Ning Wu

  2. Division of Molecular & Structural Biology, Ontario Cancer Institute/University Health Network, 610 University Avenue, Toronto, Ontario, M5G 2M9, Canada

    Ning Wu & Emil F. Pai

  3. Departments of Biochemistry, Medical Biophysics and Molecular & Medical Genetics, University of Toronto, 1 King’s College Circle, Toronto, Ontario, M5S 1A8, Canada

    Emil F. Pai

Authors
  1. Ning Wu
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  2. Emil F. Pai
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Corresponding authors

Correspondence to Ning Wu or Emil F. Pai .

Editor information

J.K. Lee

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Wu, N., Pai, E.F. Crystallographic Studies of Native and Mutant Orotidine 5′phosphate Decarboxylases. In: Lee, J. (eds) Orotidine Monophosphate Decarboxylase. Topics in Current Chemistry, vol 238. Springer, Berlin, Heidelberg. https://doi.org/10.1007/b94537

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  • DOI: https://doi.org/10.1007/b94537

  • Publisher Name: Springer, Berlin, Heidelberg

  • Print ISBN: 978-3-540-20566-1

  • Online ISBN: 978-3-540-40039-4

  • eBook Packages: Springer Book Archive

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