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The standalone aminopeptidase PepN catalyzes the maturation of blasticidin S from leucylblasticidin S Public Deposited

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https://ir.library.oregonstate.edu/concern/articles/5712m828g

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  • The peptidyl nucleoside blasticidin S (BS) isolated from Streptomyces griseochromogenes was the first non-mercurial fungicide used on a large scale to prevent rice blast. In the biosynthesis of BS, leucylblasticidin S (LBS) was suggested as the penultimate metabolite with 20-fold less inhibitory activity than the final product BS. Incomplete conversion of LBS to BS at a variable efficiency ranging from 10% to 90% was observed either in the native strain S. griseochromogenes or a heterologous producer Streptomyces lividans WJ2. In this study, we determined that maturation of BS from LBS is not a spontaneous process but is governed by a standalone peptidase PepN, which hydrolyzes LBS in a pH-sensitive way with most appropriate of pH 7~8 but is inactive when the pH is below 5 or above 10. PepN1 and PepN2, two neighboring PepN homologs from Streptomyces lividans were purified in E. coli but displayed ca.100-fold difference in LBS hydrolytic activity. Overexpression of pepN1 in WJ2 enhanced BS yield by 100% and lowered the ratio of LBS to BS from 2:1 to 2:3. This work presents the expansion of the biological role for PepN in antibiotic maturation and the first report of hydrolysis of beta amide linkage by this conserved enzyme.
  • This is the publisher’s final pdf. The published article is copyrighted by the author(s) and published by Nature Publishing Group. The published article can be found at: http://www.nature.com/articles/srep17641
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  • Yu, G., Li, L., Liu, X., Liu, G., Deng, Z., Zabriskie, M. T., ... & He, X. (2015). The standalone aminopeptidase PepN catalyzes the maturation of blasticidin S from leucylblasticidin S. Scientific Reports, 5, 17641. doi:10.1038/srep17641
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  • This work received support from the National Natural Science Foundation of China (31470195), 973 program from the Ministry of Science and Technology (2012CB721004).
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  • description.provenance : Approved for entry into archive by Patricia Black(patricia.black@oregonstate.edu) on 2016-01-13T14:55:20Z (GMT) No. of bitstreams: 3 license_rdf: 1370 bytes, checksum: cd1af5ab51bcc7a5280cf305303530e9 (MD5) ZabriskieMarkPharmacyStandaloneAminopeptidasePepN.pdf: 900661 bytes, checksum: 98e039803ce628ce51d7a34821f948a4 (MD5) ZabriskieMarkPharmacyStandaloneAminopeptidasePepN(SupplementaryMaterial).pdf: 965179 bytes, checksum: ce523e21b6b9d3722483df3f2dd99be1 (MD5)
  • description.provenance : Submitted by Patricia Black (patricia.black@oregonstate.edu) on 2016-01-13T14:54:56Z No. of bitstreams: 3 license_rdf: 1370 bytes, checksum: cd1af5ab51bcc7a5280cf305303530e9 (MD5) ZabriskieMarkPharmacyStandaloneAminopeptidasePepN.pdf: 900661 bytes, checksum: 98e039803ce628ce51d7a34821f948a4 (MD5) ZabriskieMarkPharmacyStandaloneAminopeptidasePepN(SupplementaryMaterial).pdf: 965179 bytes, checksum: ce523e21b6b9d3722483df3f2dd99be1 (MD5)
  • description.provenance : Made available in DSpace on 2016-01-13T14:55:20Z (GMT). No. of bitstreams: 3 license_rdf: 1370 bytes, checksum: cd1af5ab51bcc7a5280cf305303530e9 (MD5) ZabriskieMarkPharmacyStandaloneAminopeptidasePepN.pdf: 900661 bytes, checksum: 98e039803ce628ce51d7a34821f948a4 (MD5) ZabriskieMarkPharmacyStandaloneAminopeptidasePepN(SupplementaryMaterial).pdf: 965179 bytes, checksum: ce523e21b6b9d3722483df3f2dd99be1 (MD5) Previous issue date: 2015-12-01

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ZabriskieMarkPharmacyStandaloneAminopeptidasePepN.pdf 07/26/2017 Public
ZabriskieMarkPharmacyStandaloneAminopeptidasePepN(SupplementaryMaterial).pdf 07/26/2017 Public