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Biosynthesis of the Pseudomonas aeruginosa siderophore pyochelin :Peptide synthesis and tailoring.

Record Type:	Electronic resources : Monograph/item
Title/Author:	Biosynthesis of the Pseudomonas aeruginosa siderophore pyochelin :
Reminder of title:	Peptide synthesis and tailoring.
Author:	Patel, Hiten M.
Description:	201 p.
Notes:	Adviser: Christopher T. Walsh.
Notes:	Source: Dissertation Abstracts International, Volume: 64-05, Section: B, page: 2178.
Contained By:	Dissertation Abstracts International64-05B.
Subject:	Chemistry, Biochemistry.
Online resource:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3091655
ISBN:	0496393642

Biosynthesis of the Pseudomonas aeruginosa siderophore pyochelin :Peptide synthesis and tailoring.
Patel, Hiten M.

Biosynthesis of the Pseudomonas aeruginosa siderophore pyochelin :Peptide synthesis and tailoring. [electronic resource] - 201 p.

Adviser: Christopher T. Walsh.

Thesis (Ph.D.)--Harvard University, 2003.

Pyochelin (Pch), the tricyclic iron chelating siderophore produced as a virulence factor by Pseudomonas aeruginosa, is encoded by the NRPS Pch synthetase. The Pch system encodes for many intriguing catalytic steps including: (1) the heterocyclization of N-acyl-cysteinyl-S-enzyme intermediates to thiazolinyl rings; (2) the epimerization of the first thiazoline ring; (3) the regioselective redox adjustment of the terminal thiazoline of Pch to thiazolidine; and (4) the introduction of an N-methyl group on the terminal thiazoline ring. This work explores each of these modifications. We have fully reconstituted the pyochelin synthetase assigning all 14 chemical steps to their respective catalytic domains and have characterized three novel thiazoline tailoring activities found in PchE (epimerization), PchF (methylation), and PchG (reduction).

ISBN: 0496393642Subjects--Topical Terms:

226900
Chemistry, Biochemistry.

Biosynthesis of the Pseudomonas aeruginosa siderophore pyochelin :Peptide synthesis and tailoring.
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245 1 0 $a Biosynthesis of the Pseudomonas aeruginosa siderophore pyochelin : $b Peptide synthesis and tailoring. $h [electronic resource]
300 $a 201 p.
500 $a Adviser: Christopher T. Walsh.
500 $a Source: Dissertation Abstracts International, Volume: 64-05, Section: B, page: 2178.
502 $a Thesis (Ph.D.)--Harvard University, 2003.
520 # $a Pyochelin (Pch), the tricyclic iron chelating siderophore produced as a virulence factor by Pseudomonas aeruginosa, is encoded by the NRPS Pch synthetase. The Pch system encodes for many intriguing catalytic steps including: (1) the heterocyclization of N-acyl-cysteinyl-S-enzyme intermediates to thiazolinyl rings; (2) the epimerization of the first thiazoline ring; (3) the regioselective redox adjustment of the terminal thiazoline of Pch to thiazolidine; and (4) the introduction of an N-methyl group on the terminal thiazoline ring. This work explores each of these modifications. We have fully reconstituted the pyochelin synthetase assigning all 14 chemical steps to their respective catalytic domains and have characterized three novel thiazoline tailoring activities found in PchE (epimerization), PchF (methylation), and PchG (reduction).
520 # $a When bacteria are in iron-limited environments they often respond with the production of low molecular weight iron chelators known as siderophores, with moderate (pyochelin) to good (mycobactins) to remarkable (enterobactin) affinities for scavenging FeIII. Siderophores fall into three general types, with hydroxamates (mycobactin, aerobactin), catechols (enterobactin, vibriobactin) or thiazoline/oxazoline (pyochelin, yersiniabactin) as iron-coordinating functional groups, but all three types are assembled by polyketide synthases (PKS) and/or nonribosomal peptide synthetases (NRPS). PKSs and NRPSs comprise a class of large multimodular enzymes that catalyze the synthesis of biopolymers (e.g. vancomycin, penicillins, cyclosporins, bleomycin); through the utilization of a "thiotemplate" mechanism, these multimodular/multienzyme systems generate diverse structures derived from acyl-coenzyme A or amino acid monomers. New natural products can be generated by introducing variability into the structure through the incorporation of various monomers and the action of a diverse array of tailoring enzymes. Identification and characterization of novel peptide synthetases and tailoring enzymes allows for a better understanding of how NRPSs systems generate structural diversity. The opportunistic pathogen Pseudomonas aeruginosa makes both a high affinity peptide hydroxamate, pyoverdin and a low affinity peptide bithiazoline, pyochelin, as siderophores that contribute to pathogenicity.
590 $a School code: 0084.
650 # 0 $a Chemistry, Biochemistry. $3 226900
650 # 0 $a Biology, Microbiology. $3 226920
710 0 # $a Harvard University. $3 212445
773 0 # $g 64-05B. $t Dissertation Abstracts International
790 $a 0084
790 1 0 $a Walsh, Christopher T., $e advisor
791 $a Ph.D.
792 $a 2003
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