Overview

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 summarised in this volume.

Full Product Details

Author:   Maria Vas
Publisher:   Nova Science Publishers Inc
Imprint:   Nova Science Publishers Inc
Weight:   0.718kg
ISBN:  

9781628088366

ISBN 10:   1628088362
Pages:   309
Publication Date:   01 December 2013
Audience:   Professional and scholarly ,  College/higher education ,  Professional & Vocational ,  Postgraduate, Research & Scholarly
Format:   Hardback
Publisher's Status:   Active
Availability:   Available To Order  
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Table of Contents

Introduction; Three-Dimensional Structure as Determined by X-Ray Studies; Structural Information as Derived from Studies with Solubilised PGK; Folding Mechanism of a Two-Domain Protein as Exemplified by PGK; Physiological & Non-Physiological Functions & its Abundance; Kinetic Reaction Pathway for PGK; Anomalous Kinetic Behaviour: Activation by Anions & Excess Substrates; Antagonistic Binding of the Two Substrates; Role of the Metal-Ion in Nucleotide Binding & in the Catalysis; Architecture of the Active Site & Importance of Charge-Balance in the Catalysis; Substrate-Assisted Co-Operative Interaction of the Two Domains: Mechanism of Domain Closure at the Level of Side-Chain Interactions; Structural-Temporal Description of the Reaction Cycle; Pathological Anatomy of Phosphoglycerate Kinase; Pathological Physiology of Phosphoglycerate Kinase; Index.

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