Phosphoglycerate Kinase: A Hinge-Bending Enzyme

Maria Vas (Editor)
Professor, Institute for Enzymology, Biological Research Center, Hungarian Academy of Sciences, Budapest, Hungary

Series: Molecular Anatomy and Physiology of Proteins
BISAC: SCI008000

Clear

$205.00

Volume 10

Issue 1

Volume 2

Volume 3

Special issue: Resilience in breaking the cycle of children’s environmental health disparities
Edited by I Leslie Rubin, Robert J Geller, Abby Mutic, Benjamin A Gitterman, Nathan Mutic, Wayne Garfinkel, Claire D Coles, Kurt Martinuzzi, and Joav Merrick

eBook

Digitally watermarked, DRM-free.
Immediate eBook download after purchase.

Product price
Additional options total:
Order total:

Quantity:

Details

Phosphoglycerate kinase (PGK) is an essential metabolic enzyme for all living organisms. It catalyses the high-energy phospho-transfer reaction from 1,3-bisphosphoglycerate to the beta-phosphate of ADP and thereby produces ATP. In mammals, PGK has more widespread roles, particularly in oncogenesis and in activating anti-retroviral drugs. Namely, PGK exhibits specific thiol-reductase activity important in the inhibition of plasmin-mediated angiogenesis required for solid tumour development. The phosphorylating activity of PGK, however, has been additionally proved to be involved in specific activation of antiviral and antitumour nucleotide-analogue drugs.

In addition, the simple two-domain structure of PGK has served as a good folding-model of multidomain proteins. From folding-studies, not only the possible role of domains in the self-organisation process has been exemplified, but characteristics of the sophisticated protein misfolding mechanism has also been described. Besides the pathological anatomy (misfolding), the pathological physiology (misfunction) of PGK is also overviewed. Human phosphoglycerate kinase mutations have been identified to be associated with various serious diseases, such as mild to severe haemolytic anaemia, neurological disorders, mental retardation, behavioural aberrations, and neurological symptoms. These aspects are also discussed and summarized in this volume. (Imprint: Nova Biomedical )

Acknowledgements

Introduction

Abbreviations

Part I. NORMAL ANATOMY: STRUCTURAL FEATURES

Chapter I. Three-Dimensional Structure as Determined by X-Ray Studies

Chapter II. Structural Information as Derived from Studies with Solubilized PGK

Chapter III. Folding Mechanism of a Two-Domain Protein as Exemplified by PGK

Part II. PHYSIOLOGY: FUNCTIONAL CHARACTERISTICS

Chapter IV. Physiological and Non-Physiological Functions of PGK and Its Abundance

Chapter V. Kinetic Reaction Pathway for PGK

Chapter VI. Anomalous Kinetic Behaviour: Activation by Anions and Excess Substrates

Chapter VII. Antagonistic Binding of the Two Substrates

Chapter VIII. Role of the Metal-Ion in Nucleotide Binding and in the Catalysis

Part III: RELATIONSHIP BETWEEN STRUCTURE AND FUNCTION

Chapter IX. Architecture of the Active Site and Importance of Charge-Balance in Catalysis

Chapter X. Substrate-Assisted Cooperative Interaction of the Two Domains: Mechanism of Domain Closure at the Level of Atomic Interactions

Chapter XI. Structural-Temporal Description of the Reaction Cycle

Part IV. PATHOLOGICAL ANATOMY (MISFOLDING) AND PHYSIOLOGY (MISFUNCTION)

Chapter XII. Pathological Anatomy of PGK: Misfolding and Aggregation

Chapter XIII. Pathological Physiology of PGK

References

Index

You have not viewed any product yet.


SHOW ALL OF MY RECENTLY VIEWED BOOKS