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1 otryptophan represents a novel substrate for non-ribosomal peptide synthetases.
2 umarate:coenzyme A ligases, luciferases, and non-ribosomal peptide synthetases.
3 nisms that could enable engineering of novel non-ribosomal peptide synthetases.
5 mproved substrate specificity prediction for non-ribosomal peptide synthetase adenylation domains bas
6 ly strict substrate specificities of related non-ribosomal peptide synthetase adenylation enzymes.
7 is synthesized in part by enzymes resembling non-ribosomal peptide synthetases and that the ABC trans
10 Curacin A is a polyketide synthase (PKS)-non-ribosomal peptide synthetase-derived natural product
14 tations that upregulate transcription of the non-ribosomal peptide synthetase gene required for nidul
18 suggests that AcsD and other members of the non-ribosomal peptide synthetase-independent siderophore
20 diction software, TxtB was identified as the non-ribosomal peptide synthetase module specific for 4-n
21 ached to CmaD through the actions of CmaA, a non-ribosomal peptide synthetase module, and CmaE, an un
22 Thaxtomin A is produced by the action of two non-ribosomal peptide synthetase modules (TxtA and TxtB)
23 cluding the expected polyketide synthase and non-ribosomal peptide synthetase modules and tailoring g
24 escribe the structures of two different holo-non-ribosomal peptide synthetase modules, each revealing
25 n this model, VbsS, which is similar to many non-ribosomal peptide synthetase multienzymes, has a cen
26 e approach were applied to the known PKS and non-ribosomal peptide synthetase (NRPS) gene clusters in
27 hotransferase self-resistance gene (vph) and non-ribosomal peptide synthetase (NRPS) gene probes ampl
29 tion of specialized metabolites derived from non-ribosomal peptide synthetase (NRPS) or polyketide sy
30 study, we determined the function of a novel non-ribosomal peptide synthetase (NRPS) system carried b
32 ve combination of polyketide synthase (PKS), non-ribosomal peptide synthetase (NRPS), and shikimate p
35 -CoA synthetases, the adenylation domains of non-ribosomal peptide synthetases (NRPS), and firefly lu
37 The peptide backbone of PVD is assembled by non-ribosomal peptide synthetases (NRPSs) and modified b
38 teins termed polyketide synthases (PKSs) and non-ribosomal peptide synthetases (NRPSs) that contain r
39 y, the nocardicin A gene cluster encodes two non-ribosomal peptide synthetases (NRPSs), NocA and NocB
43 and peptide-polyketide siderophores involves non-ribosomal peptide synthetase, polyketide synthase an
44 organization of the nos synthetase, a mixed non-ribosomal peptide synthetase-polyketide synthase, is
46 s are synthesized from a classically derived non-ribosomal peptide synthetase tripeptide (from delta-
47 und that expression of nrps1 which encodes a non-ribosomal peptide synthetase was elevated in the omp
48 ding the structural basis for catalysis with non-ribosomal peptide synthetases will facilitate bioeng
49 ed by the action of polyketide synthases and non-ribosomal peptide synthetases with unusual domain st
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