Please use this identifier to cite or link to this item: https://doi.org/10.1016/S0960-894X(02)00067-7
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dc.titleSubstrate spectrum of tyrocidine thioesterase probed with randomized peptide N-acetylcysteamine thioesters
dc.contributor.authorXie, G.
dc.contributor.authorUttamchandani, M.
dc.contributor.authorChen, G.Y.J.
dc.contributor.authorBu, X.
dc.contributor.authorSan, S.L.
dc.contributor.authorKa, M.W.
dc.contributor.authorYan, W.
dc.contributor.authorYao, S.Q.
dc.contributor.authorGuo, Z.
dc.date.accessioned2014-10-16T08:42:13Z
dc.date.available2014-10-16T08:42:13Z
dc.date.issued2002-03-25
dc.identifier.citationXie, 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
dc.identifier.issn0960894X
dc.identifier.urihttp://scholarbank.nus.edu.sg/handle/10635/94965
dc.description.abstractApparent 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.
dc.description.urihttp://libproxy1.nus.edu.sg/login?url=http://dx.doi.org/10.1016/S0960-894X(02)00067-7
dc.sourceScopus
dc.typeArticle
dc.contributor.departmentCHEMISTRY
dc.description.doi10.1016/S0960-894X(02)00067-7
dc.description.sourcetitleBioorganic and Medicinal Chemistry Letters
dc.description.volume12
dc.description.issue6
dc.description.page989-992
dc.description.codenBMCLE
dc.identifier.isiut000175291700037
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