Nonribosomal Peptide and Polyketide Biosynthesis Methods and Protoco
This volume presents an overview of nonribosomal peptide synthetase (NRPS) and polyketide synthase (PKS) structure and function. It then continues with methods for the analysis of these pathways including conventional enzymological assays, contempor
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Bradley S. Evans Editor
Nonribosomal Peptide and Polyketide Biosynthesis Methods and Protocols
METHODS
IN
MOLECULAR BIOLOGY
Series Editor John M. Walker School of Life and Medical Sciences University of Hertfordshire Hatfield, Hertfordshire, AL10 9AB, UK
For further volumes: http://www.springer.com/series/7651
Nonribosomal Peptide and Polyketide Biosynthesis Methods and Protocols Editor
Bradley S. Evans Donald Danforth Plant Science Center, Saint Louis, Missouri, USA
Editor Bradley S. Evans Donald Danforth Plant Science Center Saint Louis, Missouri USA
ISSN 1064-3745 ISSN 1940-6029 (electronic) Methods in Molecular Biology ISBN 978-1-4939-3373-0 ISBN 978-1-4939-3375-4 (eBook) DOI 10.1007/978-1-4939-3375-4 Library of Congress Control Number: 2015957395 Springer New York, NY Heidelberg New York Dordrecht London © Springer Science+Business Media New York 2016 This work is subject to copyright. All rights are reserved by the Publisher, whether the whole or part of the material is concerned, specifically the rights of translation, reprinting, reuse of illustrations, recitation, broadcasting, reproduction on microfilms or in any other physical way, and transmission or information storage and retrieval, electronic adaptation, computer software, or by similar or dissimilar methodology now known or hereafter developed. The use of general descriptive names, registered names, trademarks, service marks, etc. in this publication does not imply, even in the absence of a specific statement, that such names are exempt from the relevant protective laws and regulations and therefore free for general use. The publisher, the authors and the editors are safe to assume that the advice and information in this book are believed to be true and accurate at the date of publication. Neither the publisher nor the authors or the editors give a warranty, express or implied, with respect to the material contained herein or for any errors or omissions that may have been made. Printed on acid-free paper Humana Press is a brand of Springer Springer Science+Business Media LLC New York is part of Springer Science+Business Media (www.springer.com)
Preface Nonribosomal peptide synthetases (NRPSs) and polyketide synthases (PKSs) are fascinating families of enzymes from many standpoints. These biosynthetic enzymes share a common logic with fatty acid synthases (FASs), thiotemplate-guided assembly of metabolites. The NRPSs, PKSs, and FASs can be combined in pathways (and singular enzymes) to biosynthesize hybrid molecules. They are often very large, multienzyme polypeptides that form some of the largest protein structures in the cell. These molecular assembly lines utilize complicated substrate shuttling routines to form their products from an array of over 500 documented monomer subunits. NRPS and PKS biosynthetic pathways produce a wide range of bioactive compounds from the well-known medicines penicillin, tetracycline, erythromycin, lovastatin, cyclosporine, and vancomycin, to the widely used herbicide phosphinothricin tripeptide (Bialaph
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