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Oxidative cyclizations in orthosomycin biosynthesis expand the known chemistry of an oxygenase superfamily.

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Title: Oxidative cyclizations in orthosomycin biosynthesis expand the known chemistry of an oxygenase superfamily.
Authors: McCulloch KM; Department of Pharmacology, Vanderbilt University, Nashville, TN 37232;, McCranie EK; Department of Chemistry, Vanderbilt University, Nashville, TN 37235;, Smith JA; Department of Biochemistry, Vanderbilt University, Nashville, TN 37232., Sarwar M; Department of Pharmacology, Vanderbilt University, Nashville, TN 37232;, Mathieu JL; Department of Pharmacology, Vanderbilt University, Nashville, TN 37232;, Gitschlag BL; Department of Pharmacology, Vanderbilt University, Nashville, TN 37232;, Du Y; Department of Chemistry, Vanderbilt University, Nashville, TN 37235;, Bachmann BO; Department of Chemistry, Vanderbilt University, Nashville, TN 37235; Department of Biochemistry, Vanderbilt University, Nashville, TN 37232 brian.bachmann@vanderbilt.edu tina.iverson@vanderbilt.edu., Iverson TM; Department of Pharmacology, Vanderbilt University, Nashville, TN 37232; Department of Biochemistry, Vanderbilt University, Nashville, TN 37232 brian.bachmann@vanderbilt.edu tina.iverson@vanderbilt.edu.
Source: Proceedings of the National Academy of Sciences of the United States of America [Proc Natl Acad Sci U S A] 2015 Sep 15; Vol. 112 (37), pp. 11547-52. Date of Electronic Publication: 2015 Aug 03.
Publication Type: Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.
Journal Info: Publisher: National Academy of Sciences Country of Publication: United States NLM ID: 7505876 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1091-6490 (Electronic) Linking ISSN: 00278424 NLM ISO Abbreviation: Proc Natl Acad Sci U S A Subsets: MEDLINE
Database: MEDLINE Ultimate
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  Data: Oxidative cyclizations in orthosomycin biosynthesis expand the known chemistry of an oxygenase superfamily.
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  Data: <searchLink fieldCode="AU" term="%22McCulloch+KM%22">McCulloch KM</searchLink>; Department of Pharmacology, Vanderbilt University, Nashville, TN 37232;<br /><searchLink fieldCode="AU" term="%22McCranie+EK%22">McCranie EK</searchLink>; Department of Chemistry, Vanderbilt University, Nashville, TN 37235;<br /><searchLink fieldCode="AU" term="%22Smith+JA%22">Smith JA</searchLink>; Department of Biochemistry, Vanderbilt University, Nashville, TN 37232.<br /><searchLink fieldCode="AU" term="%22Sarwar+M%22">Sarwar M</searchLink>; Department of Pharmacology, Vanderbilt University, Nashville, TN 37232;<br /><searchLink fieldCode="AU" term="%22Mathieu+JL%22">Mathieu JL</searchLink>; Department of Pharmacology, Vanderbilt University, Nashville, TN 37232;<br /><searchLink fieldCode="AU" term="%22Gitschlag+BL%22">Gitschlag BL</searchLink>; Department of Pharmacology, Vanderbilt University, Nashville, TN 37232;<br /><searchLink fieldCode="AU" term="%22Du+Y%22">Du Y</searchLink>; Department of Chemistry, Vanderbilt University, Nashville, TN 37235;<br /><searchLink fieldCode="AU" term="%22Bachmann+BO%22">Bachmann BO</searchLink>; Department of Chemistry, Vanderbilt University, Nashville, TN 37235; Department of Biochemistry, Vanderbilt University, Nashville, TN 37232 brian.bachmann@vanderbilt.edu tina.iverson@vanderbilt.edu.<br /><searchLink fieldCode="AU" term="%22Iverson+TM%22">Iverson TM</searchLink>; Department of Pharmacology, Vanderbilt University, Nashville, TN 37232; Department of Biochemistry, Vanderbilt University, Nashville, TN 37232 brian.bachmann@vanderbilt.edu tina.iverson@vanderbilt.edu.
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  Data: <searchLink fieldCode="JN" term="%227505876%22">Proceedings of the National Academy of Sciences of the United States of America</searchLink> [Proc Natl Acad Sci U S A] 2015 Sep 15; Vol. 112 (37), pp. 11547-52. <i>Date of Electronic Publication: </i>2015 Aug 03.
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