C
Christopher T. Walsh
Researcher at Stanford University
Publications - 841
Citations - 79830
Christopher T. Walsh is an academic researcher from Stanford University. The author has contributed to research in topics: Nonribosomal peptide & Active site. The author has an hindex of 139, co-authored 819 publications receiving 74314 citations. Previous affiliations of Christopher T. Walsh include Florida State University & Massachusetts Institute of Technology.
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Journal ArticleDOI
Characterization of rhodosaminyl transfer by the AknS/AknT glycosylation complex and its use in reconstituting the biosynthetic pathway of aclacinomycin A.
Catherine Leimkuhler,Micha Fridman,Tania J. Lupoli,Suzanne Walker,Christopher T. Walsh,Daniel Kahne +5 more
TL;DR: The first synthesis of TDP-L-rhodosamine is reported and it is proposed that AknT causes a conformational change in AknS that stabilizes the transition state and ultimately enhances transfer.
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Morphing peptide backbones into heterocycles.
TL;DR: The first insight is provided into the chemical structure of streptolysin S (SLS), a hemolytic toxin produced by the human pathogen Streptococcus pyogenes, which suggests widespread use of heterocyclization for altering peptide shape/flexibility and creating functional toxins.
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Chorismate aminations: partial purification of Escherichia coli PABA synthase and mechanistic comparison with anthranilate synthase
TL;DR: The first partial purification of the large subunit of Escherichia coli PABA synthase is reported, previously reported to be quantitatively inactivated in purification attempts.
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Crystallographic Evidence of Drastic Conformational Changes in the Active Site of a Flavin-Dependent N-Hydroxylase
TL;DR: In this article, the authors have shown that the piperazic acid moiety contained in the kutzneride scaffold, which is vital for its antibiotic activity, has been derived from the hydroxylated product of l-ornithine, l-N5-hydroxyORNithine.
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C-Methyltransferase and Cyclization Domain Activity at the Intraprotein PK/NRP Switch Point of Yersiniabactin Synthetase
TL;DR: This study describes the first in vitro assay of one such switch point that also involves a concomitant C-methylation of the growing acyl chain, and evaluates the catalytic capacity of the HMWP1 NRPS fourdomain module to effect the PK-to-NRP chain-switching step.