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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Studies on the kinetics and stoichiometry of inactivation of Pseudomonas omega-amino acid:pyruvate transaminase by gabaculine.
TL;DR: A homogeneous pyruvate-requiring omega-amino acid transaminase from Pseudomonas species F-126 has been examined for its behavior with gamma-aminobutyrate as omega-AMino acid substrate and for its susceptibility to the cyclic dihydroaromatic GABA analogue, gabaculine, a known suicide substrate for alpha-ketoglutarate-Requiring GABA transaminases.
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Structural Insights into Nonribosomal Peptide Enzymatic Assembly Lines
TL;DR: In this paper, the authors reviewed recent breakthrough achievements in both X-ray and NMR spectroscopic studies that illuminate the architecture of NRPS PCP domains, PCP-containing didomainfragments and of a full termination module (C-A-PCP-TE).
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The position of a key tyrosine in dTDP-4-Keto-6-deoxy-D-glucose-5-epimerase (EvaD) alters the substrate profile for this RmlC-like enzyme.
Alexandra B. Merkel,Louise L. Major,James C. Errey,Michael D. Burkart,Robert A. Field,Christopher T. Walsh,James H. Naismith +6 more
TL;DR: The high resolution structure and biochemical characterization of EvaD compared with the structures of authentic RmlC enzymes indicates that a subtle change in the enzyme active site repositions a key catalytic Tyr residue.
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Enhanced Macrocyclizing Activity of the Thioesterase from Tyrocidine Synthetase in Presence of Nonionic Detergent
TL;DR: Enhanced activity allowed enzymatic macrocyclization of a solid phase library of tyrocidine decapeptides to identify acceptable substitutions at the Orn9 position which had previously been inaccessible for diversification.
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Enzymatic Glycosylation of Vancomycin Aglycon: Completion of a Total Synthesis of Vancomycin and N- and C-Terminus Substituent Effects of the Aglycon Substrate
Atsushi Nakayama,Akinori Okano,Yiqing Feng,James C. Collins,Karen C. Collins,Christopher T. Walsh,Dale L. Boger +6 more
TL;DR: Studies on the further development of the sequential glycosylations of the vancomycin aglycon catalyzed by the Glycosyltransferases GtfE and GtfD and the observation of unusual, perhaps unexpected, agly Con substrate substituent effects on the rate and efficiency of the initial glycosYLation reaction are reported.