Mammalian heme peroxidase enzymes play a critical role in innate immune responses and disease prevention. The formation of potent chemical oxidants is essential to this protective physiologic activity in immunity. Although highly beneficial in the context of immune defense, it is now well established that peroxidases and their overproduction of oxidants contribute to the initiation and persistence of many chronic inflammatory conditions in the cardiovascular, neurologic, respiratory, renal, and gastrointestinal systems. Peroxidasins, a protein family related to heme peroxidases, play a novel role in tissue biogenesis and matrix assembly, which are also attracting attention in different pathological contexts. Given the diverse roles of mammalian heme peroxidases and the breadth and incidence of pathologies associated with these enzymes, there has been significant interest in modulating peroxidase activity as a therapeutic strategy. This book highlights recent developments in our understanding of the chemistry, biochemistry and biological roles of mammalian peroxidases and their associated oxidants, their involvement in both innate immunity and chronic inflammatory disease in a variety of end organs, and potential therapeutic approaches to modulate and prevent damaging reactions. Key Features Structure and biosynthesis of mammalian peroxidases Reactivity of hypohalous acids with biological substrates Peroxidases in innate immunity Peroxidases in human pathology Modulation of peroxidase-induced biological damage

This book will provide an up to date handbook that is unique in its combination of both the general aspects of heme protein structure and the function in a single volume.

The second of two relatively independent volumes on the chemistry and biology of peroxidases. Volumes 2 covers the peroxidases isolated from plants and microorganisms, and includes detailed discussions of some of the unique reactions catalyzed by these enzymes. Volume one covered the peroxidases isolated from animal sources, as well as the "pseudo- peroxidase activity" of prostaglandin H synthase and of myoglobin and hemoglobin. Acidic paper. Annotation copyrighted by Book News, Inc., Portland, OR

Mammalian Heme Peroxidases and Mycobacterium tuberculosis.

The Peroxidases in Chemistry and Biology series provides up-to-date information on a wide range of developments in the field of Peroxidases, methods and applications. This is Volume 1 originally published in 1990.

The last systematic description of heme peroxidases was published in 1999 by Brian Dunford, from the University of Alberta in Canada. The book Heme per- idases covers discussion on three-dimensional structure, reaction mechanism, kinetics, and spectral properties of representative enzymes from bacterial, plant, fungal, and animal origin. Since 1999, vast information on basic but also applied aspects of heme peroxidases has been generated. We believe fusion of these two aspects will bene?t research of those dedicated to development of biocatalytic process. The aim of this book is to present recent advances on basic aspects such as evolution, structure–function relation, and catalytic mechanism, as well as applied aspects, such as bioreactor and protein engineering, in order to provide the tools for rational design of enhanced biocatalysts and biocatalytic processes. The book does not include an exhaustive listing of references but rather a selected collection to enrich discussion and to allow envisioning future directions for research. This book is organized in three parts. In Part I, current knowledge of structure and mechanism of peroxidases is covered. From the molecular phylogeny, going through the in?uence of structural factors over oxidative ability to the molecular mechanism of catalysis, the authors intend to provide an understanding of per- idases at the molecular level. The understanding of the fundamental behavior of peroxidases will allow further adequation, design, and/or optimization of pero- dase-based catalysis to a particular process. In Part II, research on potential applications of peroxidases in several ?elds is presented and discussed.