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|Title:||Substrate spectrum of tyrocidine thioesterase probed with randomized peptide N-acetylcysteamine thioesters||Authors:||Xie, G.
|Issue Date:||25-Mar-2002||Citation:||Xie, G., Uttamchandani, M., Chen, G.Y.J., Bu, X., San, S.L., Ka, M.W., Yan, W., Yao, S.Q., Guo, Z. (2002-03-25). Substrate spectrum of tyrocidine thioesterase probed with randomized peptide N-acetylcysteamine thioesters. Bioorganic and Medicinal Chemistry Letters 12 (6) : 989-992. ScholarBank@NUS Repository. https://doi.org/10.1016/S0960-894X(02)00067-7||Abstract:||Apparent kinetic constants kcat and Km were determined for tyrocidine thioesterase (TycC TE) using randomized peptide N-acetylcysteamine thioesters as substrate analogues. The enzyme has been found to be adequately active for the synthesis of positional-scanning libraries for novel antibiotic screening with reduced kcat/Km in the range of 2 to 82 folds lower than that of the wild-type sequence © 2002 Elsevier Science Ltd. All rights reserved.||Source Title:||Bioorganic and Medicinal Chemistry Letters||URI:||http://scholarbank.nus.edu.sg/handle/10635/94965||ISSN:||0960894X||DOI:||10.1016/S0960-894X(02)00067-7|
|Appears in Collections:||Staff Publications|
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