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Advances in Enzymology and Related Areas of Molecular Biology / Edition 1

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Overview

This book covers important advances in enzymology, explaining the behavior of enzymes and how they can be utilized to develop novel drugs, synthesize known and novel compounds, and understand evolutionary processes. Advances in Enzymology focuses on enzymes, the primary catalysts of life processes. The explanation of the behavior of enzymes can be found via studies of their chemical mechanisms and can be utilized to develop novel drugs, synthesize known and novel compounds, and understand evolutionary processes. The transglutaminases, first described in 1957, are a large, widely-distributed family of enzymes canonically responsible for the amidation/transamidation of protein side chains. The extraordinary diversity of names associated with various enzymatic activities now recognized and aggregated as transglutaminase bears witness to the remarkable diversity of biological roles associated with the activity, including myriad human diseases.

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Editorial Reviews

From the Publisher
"With its discussion of current concepts of the biochemical basis of antibiotic resistance and its impact on modern medicine, this book will appeal to students, researchers, scientists, and clinicians interested in the areas of enzymology and mechanism of bacterial resistance." (Doody's, 26 August 2011)
Doody's Review Service
Reviewer: Omer Iqbal, MD, FACC, FESC (Loyola University Medical Center)
Description: This valuable resource on the biochemical basis of antibiotic resistance discusses recent concepts of resistance related to a complex series of multidrug efflux transporters and multidrug efflux pumps, most importantly the resistance-nodulation-division (RND) family of bacterial efflux pumps.
Purpose: Because of the extraordinary importance of antibiotic resistance in modern medicine, this book is the first of a series on recent advances in the biochemical basis of antibiotic resistance.
Audience: It is written for students and researchers in molecular biology, biochemistry, and enzymology as well as scientists interested in the discovery of an enzyme, its properties, and its applications. In my opinion, even clinicians specializing in infectious diseases would find this book of immense help.
Features: Each of the seven chapters is written by noted experts. The first chapter covers the structure and mechanism of RND-type multidrug efflux pumps considered to be the most important phenomenon of bacterial resistance, which the second chapter concentrates on the inducers of RND efflux pump activation and inhibitors of bacterial efflux pumps serving as multilevel controls. The third chapter details current concepts of the structure of tripartite RND transporters vital to the pathogenicity of important human pathogens such as Escherichia coli, Campylobacter, and Neisseria. The fourth chapter covers the largest and structurally most diverse group of secondary membrane transport proteins, the major facilitator superfamily (MFS) group, and its role in the pathogenicity of gram-positive and gram-negative bacteria, while the fifth chapter discusses efflux pumps as an important mechanism for quinolone resistance. The sixth chapter is a genomic update on xenobiotic efflux in bacteria and fungi. The last chapter provides a survey of oxidative paracatalytic reactions catalyzed by enzymes that generate carbanionic intermediates and the implications for ROS production, cancer etiology, and neurodegenerative diseases. The book is well illustrated with both black-and-white and color illustrations.
Assessment: With its discussion of current concepts of the biochemical basis of antibiotic resistance and its impact on modern medicine, this book will appeal to students, researchers, scientists, and clinicians interested in the areas of enzymology and mechanism of bacterial resistance.
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Product Details

Meet the Author

Eric J. Toone, PhD, is Professor of Chemistry and Professor of Biochemistry at Duke University. He holds numerous patents and has written extensively on physical organic and biophysical chemistry. Professor Toone has served as a member of the Bioorganic and Natural Products Study Section at the National Institutes of Health, and is currently a member of the NSERC Organic & Inorganic Review panel (Canada). Professor Toone is the Deputy Director for the Advanced Research Projects Agency—Energy (ARPA-E) of the Department of Energy and directs ARPA-E's electrofuels program.

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Table of Contents

Contributors vii

Preface ix

Structure and Regulation of Type 2 Transglutaminase in Relation to Its Physiological Functions and Pathological Roles 1
Carlo M. Bergamini, Russell J. Collighan, Zhuo Wang, and Martin Griffin

Physiopathological Roles of Human Transglutaminase 2 47
Vittorio Gentile

Transglutaminase in Epidermis and Neurological Disease or What Makes a Good Cross-Linking Substrate 97
Guylaine Hoffner, Amandine VanHoutteghem, William Andre, and Philippe Djian

Transglutaminase 2: A New Paradigm for NF-B Involvement in Disease 161
Soo-Youl Kim

Transglutaminase 2 At the Crossroads between Cell Death and Survival 197
Mauro Piacentini, Manuela D’Eletto, Laura Falasca, Maria Grazia Farrace, and Carlo Rodolfo

Tissue Transglutaminase and Its Role in Human Cancer Progression 247
Bo Li, Richard A. Cerione, and Marc Antonyak

Transglutaminase 2 Dysfunctions in the Development of Autoimmune Disorders: Celiac Disease and TG2−/−Mouse 295
Zsuzsa Szondy, Ilma Korponay-Szabo, Robert Kiraly, and Laszlo Fesus

Effects and Analysis of Transglutamination on Protein Aggregation and Clearance in Neurodegenerative Diseases 347
Zoltan Nemes

Transglutaminase-Mediated Remodeling of the Human Erythrocyte Membrane Skeleton: Relevance for Erythrocyte Diseases with Shortened Cell Lifespan 385
Laszlo Lorand, S. N. Prasanna Murthy, Anwar A. Khan, Weihua XUE, Oksana Lockridge, and Athar H. Chishti

Irreversible Inhibitors of Tissue Transglutaminase 415
Jeffrey W. Keillor, Nicolas Chabot, Isabelle Roy, Amina Mulani, Olivier Leogane, and Christophe Pardin

Methionine Adenosyltransferase (S-Adenosylmethionine Synthetase) 449
Marıa A. Pajares and George D. Markham

Index 523

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