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Functional Analysis of A Pyoverdine Synthetase from Pseudomonas sp. MIS38
Title: | Functional Analysis of A Pyoverdine Synthetase from Pseudomonas sp. MIS38 |
Authors: | LIM, Siew Ping Browse this author | ROONGSAWANG, Niran Browse this author | WASHIO, Kenji Browse this author →KAKEN DB | MORIKAWA, Masaaki Browse this author →KAKEN DB |
Keywords: | fluorescent Pseudomonas | pyoverdine synthetase | nonribosomal peptide | gene disruption | arthrofactin |
Issue Date: | Aug-2007 |
Publisher: | Japan Society for Bioscience, Biotechnology, and Agrochemistry |
Journal Title: | Bioscience, Biotechnology, and Biochemistry |
Volume: | 71 |
Issue: | 8 |
Start Page: | 2002 |
End Page: | 2009 |
Publisher DOI: | 10.1271/bbb.70185 |
PMID: | 17690457 |
Abstract: | Fluorescent Pseudomonas sp. MIS38 produces a cyclic lipopeptide, arthrofactin. Arthrofactin is synthesized by a unique nonribosomal peptide synthetase (NRPS) with dual C/E-domains. In this study, another class of cyclic peptide, pyoverdine, was isolated from MIS38, viz., Pvd38. The main fraction of Pvd38 had an m⁄z value of 1,064.57 and contained Ala, Glu, Gly, (OHOrn), Ser, and Thr at a ratio of 2:1:1:(1):1:1 in the peptide part, suggesting a new structure compound. A gene encoding NRPS for the chromophore part of Pvd38 was identified, and we found that it contained a conventional E-domain. Gene disruption completely impaired the production of Pvd38, demonstrating that the synthetase is functional. This observation allows us to conclude that different NRPS systems with dual C/E-domains (in arthrofactin synthetase) and a conventional E-domain (in pyoverdine synthetase) are both functional in MIS38. |
Relation: | http://www.jstage.jst.go.jp/ |
Type: | article |
URI: | http://hdl.handle.net/2115/29888 |
Appears in Collections: | 環境科学院・地球環境科学研究院 (Graduate School of Environmental Science / Faculty of Environmental Earth Science) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)
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Submitter: 森川 正章
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