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2 Oxoglutarate Dependent Oxygenases (Rsc Metallobiology Series, 3, Band 3) - Hardcover

 
9781849739504: 2 Oxoglutarate Dependent Oxygenases (Rsc Metallobiology Series, 3, Band 3)
Hardcover
ISBN 10: 1849739501 ISBN 13: 9781849739504
Verlag: Royal Society of Chemistry, 2015

Inhaltsangabe

Since the discovery of the first examples of 2-oxoglutarate-dependent oxygenase-catalysed reactions in the 1960s, a remarkably broad diversity of alternate reactions and substrates has been revealed, and extensive advances have been achieved in our understanding of the structures and catalytic mechanisms. These enzymes are important agrochemical targets and are being pursued as therapeutic targets for a wide range of diseases including cancer and anemia.
This book provides a central source of information that summarizes the key features of the essential group of 2-oxoglutarate-dependent dioxygenases and related enzymes. Given the numerous recent advances and biomedical interest in the field, this book aims to unite the latest research for those already working in the field as well as to provide an introduction for those newly approaching the topic, and for those interested in translating the basic science into medicinal and agricultural benefits.
The book begins with four broad chapters that highlight critical aspects, including an overview of possible catalytic reactions, structures and mechanisms. The following seventeen chapters focus on carefully selected topics, each written by leading experts in the area. Readers will find explanations of rapidly evolving research, from the chemistry of isopenicillin N synthase to the oxidation mechanism of 5-methylcytosine in DNA by ten-eleven-translocase oxygenases.

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Von der hinteren Coverseite

Since the discovery of the first examples of 2-oxoglutarate-dependent oxygenase-catalysed reactions in the 1960s, a remarkably broad diversity of alternate reactions and substrates has been revealed, and extensive advances have been achieved in our understanding of the structures and catalytic mechanisms. These enzymes are important agrochemical targets and are being pursued as therapeutic targets for a wide range of diseases including cancer and anemia.
This book provides a central source of information that summarizes the key features of the essential group of 2-oxoglutarate-dependent dioxygenases and related enzymes. Given the numerous recent advances and biomedical interest in the field, this book aims to unite the latest research for those already working in the field as well as to provide an introduction for those newly approaching the topic, and for those interested in translating the basic science into medicinal and agricultural benefits.
The book begins with four broad chapters that highlight critical aspects, including an overview of possible catalytic reactions, structures and mechanisms. The following seventeen chapters focus on carefully selected topics, each written by leading experts in the area. Readers will find explanations of rapidly evolving research, from the chemistry of isopenicillin N synthase to the oxidation mechanism of 5-methylcytosine in DNA by ten-eleven-translocase oxygenases.

Aus dem Klappentext

Since the discovery of the first examples of 2-oxoglutarate-dependent oxygenase-catalysed reactions in the 1960s, a remarkably broad diversity of alternate reactions and substrates has been revealed, and extensive advances have been achieved in our understanding of the structures and catalytic mechanisms. These enzymes are important agrochemical targets and are being pursued as therapeutic targets for a wide range of diseases including cancer and anemia.
This book provides a central source of information that summarizes the key features of the essential group of 2-oxoglutarate-dependent dioxygenases and related enzymes. Given the numerous recent advances and biomedical interest in the field, this book aims to unite the latest research for those already working in the field as well as to provide an introduction for those newly approaching the topic, and for those interested in translating the basic science into medicinal and agricultural benefits.
The book begins with four broad chapters that highlight critical aspects, including an overview of possible catalytic reactions, structures and mechanisms. The following seventeen chapters focus on carefully selected topics, each written by leading experts in the area. Readers will find explanations of rapidly evolving research, from the chemistry of isopenicillin N synthase to the oxidation mechanism of 5-methylcytosine in DNA by ten-eleven-translocase oxygenases.

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2-Oxoglutarate-Dependent Oxygenases

By Robert P. Hausinger, Christopher J. Schofield

The Royal Society of Chemistry

Copyright © 2015 The Royal Society of Chemistry
All rights reserved.
ISBN: 978-1-84973-950-4

Contents

Chapter 1 Biochemical Diversity of 2-Oxoglutarate-Dependent Oxygenases Robert P. Hausinger, 1, 
Chapter 2 Introduction to Structural Studies on 2-Oxoglutarate-Dependent Oxygenases and Related Enzymes Wei Shen Aik, Rasheduzzaman Chowdhury, Ian J. Clifton, Richard J. Hopkinson, Thomas Leissing, Michael A. McDonough, Radoslaw Nowak, Christopher J. Schofield, and Louise J. Walport, 59, 
Chapter 3 Mechanisms of 2-Oxoglutarate-Dependent Oxygenases: The Hydroxylation Paradigm and Beyond J. Martin Bollinger Jr., Wei-chen Chang, Megan L. Matthews, Ryan J. Martinie, Amie K. Boal, and Carsten Krebs, 95, 
Chapter 4 Synthetic Models of 2-Oxoglutarate-Dependent Oxygenases Caleb J. Allpress, Scott T. Kleespies, and Lawrence Que Jr, 123, 
Chapter 5 Collagen Hydroxylases Johanna Myllyharju, 149, 
Chapter 6 The Role of 2-Oxoglutarate-Dependent Oxygenases in Hypoxia Sensing Sarah E. Wilkins, Emily Flashman, John S. Scotti, Richard J. Hopkinson, Rasheduzzaman Chowdhury, and Christopher J. Schofield, 169, 
Chapter 7 JmjC Lysine Demethylases Xiaodong Cheng and Raymond C. Trievel, 210, 
Chapter 8 AlkB and Its Homologues – DNA Repair and Beyond Tina A. Müller and Robert P. Hausinger, 246, 
Chapter 9 RNA Demethylation by FTO and ALKBH5 Guanqun Zheng and Chuan He, 263, 
Chapter 10 Role of ALKBH8 in the Synthesis of Wobble Uridine Modifications in tRNA Pål Ø. Falnes and Angela Yeuan Yen Ho, 275, 
Chapter 11 The TET/JBP Family of Nucleic Acid Base-Modifying 2-Oxoglutarate and Iron-Dependent Dioxygenases L. Aravind, Dapeng Zhang, and Lakshminarayan M. Iyer, 289, 
Chapter 12 2-Oxoglutarate-Dependent Hydroxylases Involved in DNA Base J ([β-D-Glucopyranosyloxymethyluracil) Synthesis David Reynolds, Laura Cliffe, and Robert Sabatini, 309, 
Chapter 13 Dioxygenases of Carnitine Biosynthesis: 6-N-Trimethyllysine and γ-Butyrobetaine Hydroxylases Frédéric M. Vaz and Naomi van Vlies, 324, 
Chapter 14 Phytanoyl-CoA Hydroxylase: A 2-Oxoglutarate-Dependent Dioxygenase Crucial for Fatty Acid Alpha-Oxidation in Humans Ronald J. A. Wanders, Sacha Ferdinandusse, Merel S. Ebberink, and Hans R. Waterham, 338, 
Chapter 15 Role of 2-Oxoglutarate-Dependent Oxygenases in Flavonoid Metabolism Stefan Martens and Ulrich Matern, 350, 
Chapter 16 Gibberellin Metabolism Peter Hedden and Andrew L. Phillips, 367, 
Chapter 17 2-Oxoglutarate-Dependent Oxygenases of Cephalosporin Synthesis Inger Andersson and Karin Valegård, 385, 
Chapter 18 Recent Advances in the Structural and Mechanistic Biology of Non-Haem Fe(ii), 2-Oxoglutarate and O2-Dependent Halogenases Janet L. Smith and Dheeraj Khare, 401, 
Chapter 19 Isopenicillin N Synthase Peter J. Rutledge, 414, 
Chapter 20 1-Aminocyclopropane-1-Carboxylic Acid Oxidase A. Jalila Simaan and Marius Réglier, 425, 
Chapter 21 4-Hydroxyphenylpyruvate Dioxygenase and Hydroxymandelate Synthase: 2-Oxo Acid-Dependent Oxygenases of Importance to Agriculture and Medicine, 438, 
Subject Index, 458,


CHAPTER 1

Biochemical Diversity of 2-Oxoglutarate-Dependent Oxygenases

ROBERT P. HAUSINGER


1.1 Introduction

This chapter summarizes the diverse array of biochemical transformations that are catalysed by Fe(II)- and 2-oxoglutarate (2OG, also known as α-ketoglutarate)-dependent oxygenases. As described more comprehensively in Chapter 2, most of these enzymes coordinate their active site metal at one end of a double-stranded β-helix fold (Figure 1.1A) using a 2-His-1-carboxylate motif, bind 2OG within the core, and interact with their primary substrates using less conserved regions of the core and additional loops. Most representatives of this enzyme family catalyse hydroxylation reactions (Figure 1.1B), but desaturation, ring formation, ring expansion, halogenation and other types of chemistry are known, as described for several examples in later sections of this chapter. The mechanisms of these enzymes are detailed in Chapter 3, supported by chemical model investigations summarized in Chapter 4. A highly simplified mechanistic scheme for hydroxylases based on investigations of TauD (taurine hydroxylase), a well-characterized taurine-degrading enzyme (see Section 1.6.4), is depicted in Figure 1.1C. As illustrated, the binding of 2OG displaces two waters from an octahedral Fe(II) site (converting state a to state b); a third water is lost as the primary substrate binds (generating state c); the newly vacant coordination site is used to react with O2 to form an Fe(III)–superoxo species (state d); oxidative decarboxylation of 2OG yields an Fe(IV)–oxo species (state e, also known as the ferryl intermediate); this powerful oxidant abstracts a hydrogen atom from the substrate to generate a radical and Fe(III)–hydroxide (state f); and hydroxyl radical rebound (or more complex chemistry) completes substrate hydroxylation and recycles the enzyme to the initial Fe(II) state. Such enzymes are dioxygenases because both atoms of oxygen are incorporated into substrates, with one atom ending up in succinate and the second in the hydroxylated product (which decomposes spontaneously in some reactions). These enzymes are correctly referred to as primary substrate:2OG dioxygenases or primary substrate hydroxylases; it is incorrect to cite these enzymes as primary substrate dioxygenases or 2OG dioxygenases because these names imply both atoms of oxygen become incorporated into a single substrate. The other types of chemistries associated with this family of enzymes are also likely to utilize the Fe(IV)-oxo intermediate.

The total number of 2OG-dependent oxygenases found in biology is immense. For example, humans and other animals are thought to possess about 80 such enzymes. Even more are predicted to be present in plants such as the model organism Arabidopsis thaliana. Some 2OG-dependent oxygenases are widely distributed throughout aerobic life forms, whereas highly specialized enzymatic catalysts have evolved in various microorganisms or plants for synthesis or degradation of compounds found in their unique niches. In the following sections, the vast array of reactions catalysed by 2OG-dependent oxygenases are divided into seven categories. Section 1.2 describes the 2OG-dependent enzymes acting on proteins. These reactions may lead to structural consequences, have oxygen-sensing functions, alter histone properties, or possess other roles. Section 1.3 summarizes the metabolism of 2OG-dependent oxygenases acting on polynucleotides. The functions of these enzymes include DNA or RNA repair of alkylation damage, roles in transcriptional regulation, biosynthesis of base J in DNA or of specific tRNAs, and demethylation of 5-methylcytosine. Enzymes involved in lipid-related metabolism are discussed in Section 1.4. Examples include reactions related to carnitine biosynthesis, the degradation of phytanic acids, and the decoration of ornithine lipids or lipid A. Plant-specific representatives and close relatives are highlighted in Section 1.5. Of interest are reactions related to synthesis of flavonoids and anthocyanins, gibberellins, alkaloids, and other metabolites found predominantly in plants. Section 1.6 covers enzymes that act on a variety of small molecules including free amino acids, nucleobases or nucleosides, herbicides, sulfonates/sulfates and phosphonates. In some cases, the...

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Verlag
Royal Society of Chemistry
Erscheinungsdatum
2015
Sprache
Englisch
ISBN 10 
1849739501
ISBN 13 
9781849739504
Einband
Gebundene Ausgabe
Anzahl der Seiten
487
Herausgeber
Hausinger Robert P., Schofield Christopher J.
Kontakt zum Hersteller
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Verantwortliche Person
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