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1 ld better therapeutic index than the natural tyrocidine.
2 on of an alkyne handle at position 1 or 4 of tyrocidine A allowed site-selective one-step fluorescent
3                      A 400-member library of tyrocidine A analogues was synthesized on TentaGel macro
4 eptide thioester with the native sequence of tyrocidine A and can additionally cyclize peptide analog
5 sis was developed and utilized to synthesize tyrocidine A and its glycosylated derivatives.
6          Biological studies of the synthetic tyrocidine A derivatives showed that linking glycans dir
7 nking glycans directly to the Asn residue of tyrocidine A diminished its antibacterial activity, but
8 yclic beta-hairpin antimicrobial decapeptide tyrocidine A, (Tyrc A) was substituted with the d-Phe-2-
9 decapeptide-thioester to form the antibiotic tyrocidine A, and can catalyse pentapeptide-thioester di
10 rting from the cyclic decapeptide antibiotic tyrocidine A, this chemoenzymatic approach allows us to
11 for the production of the cyclic decapeptide tyrocidine A, TycC TE, retains autonomous ability to cat
12 ogen bonds analogous to those in the product tyrocidine A.
13 er to form the cyclic decapeptide antibiotic tyrocidine A.
14 irectly against bacterial cells identified a tyrocidine analogue of improved antibacterial activity.
15 ep fluorescent labeling of the corresponding tyrocidine analogues by Cu(I)-catalyzed alkyne-azide cyc
16  domain that unites the first two modules of tyrocidine biosynthesis and report the high-resolution c
17 ocidine synthetase, 13 head-to-tail cyclized tyrocidine derivatives were obtained with one to three p
18            The cyclic decapeptide antibiotic tyrocidine has D-Phe residues at positions 1 and 4, prod
19 osomal peptides (NRP) such as the antibiotic tyrocidine have D-amino acids, introduced by epimerase (
20 t are dramatically different from the native tyrocidine linear precursor.
21 hioesterase (TE) domain from the multidomain tyrocidine nonribosomal peptide synthetase (NRPS) was re
22  we show that the excised TE domain from the tyrocidine NRPS can be used to generate an array of size
23 ults demonstrate that the TE domain from the tyrocidine NRPS can catalyze cyclization of depsipeptide
24     The excised thioesterase domain from the tyrocidine NRPS has been shown to catalyze the cyclizati
25 he initial Phe-loading adenylation domain of tyrocidine synthetase completely switches the specificit
26 re we report that the excised TE domain from tyrocidine synthetase efficiently catalyses cyclization
27 iction and establish that the C(5) domain of tyrocidine synthetase is indeed (D)C(L), the apoT (thiol
28 strate that the first condensation domain of tyrocidine synthetase shows low selectivity at the donor
29  This specificity profile indicates that the tyrocidine synthetase TE, and by analogy many other TE d
30 g a thioesterase domain from the decapeptide tyrocidine synthetase, 13 head-to-tail cyclized tyrocidi
31                           In a reconstituted tyrocidine synthetase, the W227S point mutation permitte