Lasso peptides : (Record no. 8668)

MARC details
000 -LEADER
fixed length control field 03337cam a22002537i 4500
008 - FIXED-LENGTH DATA ELEMENTS--GENERAL INFORMATION
fixed length control field 140414s2015 nyua b 000 0 eng c
020 ## - INTERNATIONAL STANDARD BOOK NUMBER
ISBN 9781493910090 - pbk
100 1# - MAIN ENTRY--AUTHOR
Author Li, Yanyan
245 10 - TITLE STATEMENT
Title Lasso peptides :
Remainder of title bacterial strategies to make and maintain bioactive entangled scaffolds /
Statement of responsibility, etc Yanyan Li, Séverine Zirah, Sylvie Rebuffat.
260 ## - PUBLICATION, DISTRIBUTION, ETC. (IMPRINT)
Place of publication New York :
Name of publisher Springer,
Date of publication 2015
300 ## - COLLATION
Pagination xiii, 103 p., illus.,
Other physical details includes references
440 ## - SERIES STATEMENT/ADDED ENTRY--TITLE
Series Title Springer Briefs in microbiology
520 ## - SUMMARY, ETC.
Summary, etc Lasso peptides form a growing family of fascinating ribosomally-synthesized and post-translationally modified peptides produced by bacteria. They contain 15 to 24 residues and share a unique interlocked topology that involves an N-terminal 7 to 9-residue macrolactam ring where the C-terminal tail is threaded and irreversibly trapped. The ring results from the condensation of the N-terminal amino group with a side-chain carboxylate of a glutamate at position 8 or 9, or an aspartate at position 7, 8 or 9. The trapping of the tail involves bulky amino acids located in the tail below and above the ring and/or disulfide bridges connecting the ring and the tail. Lasso peptides are subdivided into three subtypes depending on the absence (class II) or presence of one (class III) or two (class I) disulfide bridges. The lasso topology results in highly compact structures that give to lasso peptides an extraordinary stability towards both protease degradation and denaturing conditions. Lasso peptides are generally receptor antagonists, enzyme inhibitors and/or antibacterial or antiviral (anti-HIV) agents. The lasso scaffold and the associated biological activities shown by lasso peptides on different key targets make them promising molecules with high therapeutic potential. Their application in drug design has been exemplified by the development of an integrin antagonist based on a lasso peptide scaffold. The biosynthesis machinery of lasso peptides is therefore of high biotechnological interest, especially since such highly compact and stable structures have to date revealed inaccessible by peptide synthesis. Lasso peptides are produced from a linear precursor LasA, which undergoes a maturation process involving several steps, in particular cleavage of the leader peptide and cyclization. The post-translational modifications are ensured by a dedicated enzymatic machinery, which is composed of an ATP-dependent cysteine protease (LasB) and a lactam synthetase (LasC) that form an enzymatic complex called lasso synthetase. Microcin J25, produced by Escherichia coli AY25, is the archetype of lasso peptides and the most extensively studied. To date only around forty lasso peptides have been isolated, but genome mining approaches have revealed that they are widely distributed among Proteobacteria and Actinobacteria, particularly in Streptomyces, making available a rich resource of novel lasso peptides and enzyme machineries towards lasso topologies
650 #0 - TRACINGS
Main Subject 1. Peptides
Subdivision (2nd) Structure.
650 #0 - TRACINGS
Main Subject 2. Peptides
Subdivision (2nd) Synthesis.
650 #0 - TRACINGS
Main Subject 3. Peptides
Subdivision (2nd) Physiological effect.
650 #0 - TRACINGS
Main Subject 4. Bacteria
Subdivision (2nd) Physiology.
650 12 - TRACINGS
Main Subject 5. Bacterial Proteins
Subdivision (2nd) physiology.
700 1# - ADDITIONAL AUTHOR
Additional Author Zirah, Séverine,
700 1# - ADDITIONAL AUTHOR
Additional Author Rebuffat, Sylvie,
942 ## - ADDED ENTRY ELEMENTS (KOHA)
Item type Books
050 00 - LIBRARY OF CONGRESS CALL NUMBER
Classification number QP552.P4
Item number L5 2015
082 00 - DEWEY DECIMAL CLASSIFICATION NUMBER
Classification number 612/.01575
Holdings
Source of classification or shelving scheme Not for loan Permanent location Current location Shelving location Date acquired Accession No. Full call number Barcode. Copy number Koha item type
Library of Congress Classification   Kwara State University Library Kwara State University Library Main Library 2022-10-11 018932 - 01 QP552.P4 .L5 2015 018932 - 01 01 Books
Library of Congress Classification   Kwara State University Library Kwara State University Library Main Library 2022-10-11 018932 - 02 QP552.P4 .L5 2015 018932 - 02 02 Books