2012 Fiscal Year Final Research Report
Improvement of the membrane permeability of compounds used by streptothricin biosynthetic enzymes
Project/Area Number |
22688007
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Research Category |
Grant-in-Aid for Young Scientists (A)
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Allocation Type | Single-year Grants |
Research Field |
Applied microbiology
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Research Institution | Fukui Prefectural University |
Principal Investigator |
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Project Period (FY) |
2010 – 2012
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Keywords | NRPS / ペプチド合成酵素 |
Research Abstract |
The streptothricin (ST) antibiotics, produced by Streptomyces bacteria, contain L-β-lysine oligopeptides as pendant chains. In this study, we identified three unusual nonribosomal peptide synthetases (NRPSs) involved in ST biosynthesis: ORF 5 (a stand-alone adenylation (A) domain), ORF 18 (containing thiolation (T) and condensation (C) domains) and ORF 19 (a stand-alone A domain).
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[Journal Article] A stand-alone adenylation domain forms amide bonds in streptothricin biosynthesis2012
Author(s)
Chitose Maruyama, Junya Toyoda, YasYasuo Kato, Miho Izumikawa, Motoki TakYasuo Kato, Miho Izumikawa, Motoki Takagi, Kazuo Shin-ya, Hajime Katano, Takashi Utagawa, and Yoshimitsu Hamano
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Journal Title
Nature Chem. Biol
Volume: 8
Pages: 791-797
DOI
Peer Reviewed
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