H
Hiten M. Patel
Researcher at Harvard University
Publications - 22
Citations - 801
Hiten M. Patel is an academic researcher from Harvard University. The author has contributed to research in topics: Chemistry & Medicine. The author has an hindex of 7, co-authored 7 publications receiving 680 citations.
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Journal ArticleDOI
Tailoring enzymes that modify nonribosomal peptides during and after chain elongation on NRPS assembly lines
Christopher T. Walsh,Huawei Chen,Thomas A. Keating,Brian K. Hubbard,Heather C. Losey,Lusong Luo,C. Gary Marshall,Deborah Ann Miller,Hiten M. Patel +8 more
TL;DR: Nonribosomal peptide synthetases are large enzyme complexes that synthesize a variety of peptide natural products through a thiotemplated mechanism.
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Essential PchG-Dependent Reduction in Pyochelin Biosynthesis of Pseudomonas aeruginosa
TL;DR: This study completes the identification of the biosynthetic genes required for pyochelin formation from chorismate in P. aeruginosa and attributed a reductase function to PchG.
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Assembly of the Pseudomonas aeruginosa nonribosomal peptide siderophore pyochelin: In vitro reconstitution of aryl-4, 2-bisthiazoline synthetase activity from PchD, PchE, and PchF.
TL;DR: Three Pseudomonas aeruginosa proteins involved in biogenesis of the nonribosomal peptide siderophore pyochelin, PchE, and PchF, have been expressed in and purified from Escherichia coli and are found to produce the tricyclic acid hydroxyphenyl-thiazolyl- thiazolinyl-carboxylic acid (HPTT-COOH).
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In Vitro Reconstitution of the Pseudomonas aeruginosa Nonribosomal Peptide Synthesis of Pyochelin: Characterization of Backbone Tailoring Thiazoline Reductase and N-Methyltransferase Activities†
TL;DR: Full reconstitution of the nonribosomal peptide synthetase assembly line by purified protein components has been obtained for production of this tandem bisheterocyclic siderophore during iron starvation.
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Epimerization of an L-cysteinyl to a D-cysteinyl residue during thiazoline ring formation in siderophore chain elongation by pyochelin synthetase from Pseudomonas aeruginosa.
TL;DR: It is reported that the PchE subunit of the PCh synthetase exchanges solvent deuterium into the C(2) center of the thiazoline moieties during siderophore chain elongation, suggesting a default role for MT domains of NRPS assembly lines in generating alpha-carbanionic species from thioester intermediates during sidingophoreChain elongation.