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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

Atp/gtp hydrolysis is required for oxazole and thiazole biosynthesis in the peptide antibiotic microcin b17

TL;DR: In the maturation of the Escherichia coli antibiotic Microcin B17, the product of the mcbA gene is modified posttranslationally by the multimeric Microcin synthetase complex (composed of McbB, C, and D) to cyclize four Cys and four Ser residues to four thiazoles and four oxazoles, respectively as discussed by the authors.
Journal ArticleDOI

Characterization of cyclo-acetoacetyl-L-tryptophan dimethylallyltransferase in cyclopiazonic acid biosynthesis: substrate promiscuity and site directed mutagenesis studies.

TL;DR: It is demonstrated that CpaD discriminates against free Trp but accepts tryptophan-containing thiohydantoins, diketopiperazines, and linear peptides as substrates for C4-prenylation and also acts as regiospecific O-dimethylallyltransferase (DMAT) on a tyrosine-derived tetramic acid.
Journal ArticleDOI

The posttranslational modification cascade to the thiopeptide berninamycin generates linear forms and altered macrocyclic scaffolds

TL;DR: Berninamycin is a member of the pyridine-containing thiopeptide class of antibiotics that undergoes massive posttranslational modifications from ribosomally generated preproteins.
Book ChapterDOI

Suicide substrates for flavoprotein enzymes.

TL;DR: This chapter focuses on the suicide substrates for flavoprotein enzymes, which contain activated halides, such as α-haloketone or sulfonyl halide group, which are good alkylating agents of nucleophiles not necessarily at the active site of the target enzyme.
Journal ArticleDOI

In vivo processing and antibiotic activity of microcin B17 analogs with varying ring content and altered bisheterocyclic sites

TL;DR: Antibiotic activity correlates with the number of rings and is differentially sensitive to both the location and the identity of the 4,2-tandem heterocycle pairs in MccB17, which might be useful pharmacophores in combinatorial libraries.