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Sökning: WFRF:(Borriss R.)

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1.
  • Medema, M. H., et al. (författare)
  • Minimum Information about a Biosynthetic Gene cluster
  • 2015
  • Ingår i: Nature Chemical Biology. - : Springer Science and Business Media LLC. - 1552-4450 .- 1552-4469. ; 11:9, s. 625-631
  • Forskningsöversikt (refereegranskat)abstract
    • A wide variety of enzymatic pathways that produce specialized metabolites in bacteria, fungi and plants are known to be encoded in biosynthetic gene clusters. Information about these clusters, pathways and metabolites is currently dispersed throughout the literature, making it difficult to exploit. To facilitate consistent and systematic deposition and retrieval of data on biosynthetic gene clusters, we propose the Minimum Information about a Biosynthetic Gene cluster (MIBiG) data standard.
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2.
  • Borriss, R., et al. (författare)
  • Enzymatic synthesis of 4-methylumbelliferyl (1 -> 3)-beta-D-glucooligosaccharides - new substrates for beta-1,3-1,4-D-glucanase
  • 2003
  • Ingår i: Carbohydrate Research. - : Elsevier BV. - 0008-6215 .- 1873-426X. ; 338:14, s. 1455-1467
  • Tidskriftsartikel (refereegranskat)abstract
    • The transglycosylation reactions catalyzed by beta-1,3-D-glucanases (laminaranases) were used to synthesize a number of 4-methylumbelliferyl (MeUmb) (1 --> 3)-beta-D-gluco-oligosaccharides having the common structure [beta-D-Glcp-(1 --> 3)](n)-beta-D-Glcp-MeUmb, where n = 1-5. The beta-1,3-D-glucanases used were purified from the culture liquid of Oerskovia sp. and from a homogenate of the marine mollusc Spisula sachalinensis. Laminaran and curdlan were used as (1 --> 3)-beta-D-glucan donor substrates, while MeUmb-beta-D-glucoside (MeUmbGlcp) was employed as a transglycosylation acceptor. Modification of [beta-D-Glcp-(1 --> 3)](2)-beta-D-Glcp-MeUmb (MeUmbG(3)) gives 4,6-O-benzylidene-D-glucopyranosyl or 4,6-O-ethylidene-D-glucopyranosyl groups at the non-reducing end of artificial oligosaccharides. The structures of all oligosaccharides obtained were solved by H-1 and C-13 NMR spectroscopy and electrospray tandem mass spectrometry. The synthetic oligosaccharides were shown to be substrates for a beta-1,3-1,4-D-glucanase from Rhodothermus marinus, which releases MeUmb from beta-di- and beta-triglucosides and from acetal-protected beta-triglucosides. When acting upon substrates with d.p. > 3, the enzyme exhibits an endolytic activity, primarily cleaving off MeUrnbGlcP and MeUmbG(2).
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