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Oxidative cyclization of prodigiosin by an alkylglycerol monooxygenase-like enzyme.
de Rond, Tristan; Stow, Parker; Eigl, Ian; Johnson, Rebecca E; Chan, Leanne Jade G; Goyal, Garima; Baidoo, Edward E K; Hillson, Nathan J; Petzold, Christopher J; Sarpong, Richmond; Keasling, Jay D.
Afiliação
  • de Rond T; Department of Chemistry, University of California, Berkeley, California, USA.
  • Stow P; Department of Chemistry, University of California, Berkeley, California, USA.
  • Eigl I; Department of Chemical and Biomolecular Engineering, University of California, Berkeley, California, USA.
  • Johnson RE; Department of Chemistry, University of California, Berkeley, California, USA.
  • Chan LJG; DOE Joint BioEnergy Institute, Emeryville, California, USA.
  • Goyal G; Biological Systems and Engineering Division, Lawrence Berkeley National Lab, Berkeley, California, USA.
  • Baidoo EEK; DOE Joint BioEnergy Institute, Emeryville, California, USA.
  • Hillson NJ; Biological Systems and Engineering Division, Lawrence Berkeley National Lab, Berkeley, California, USA.
  • Petzold CJ; DOE Joint BioEnergy Institute, Emeryville, California, USA.
  • Sarpong R; Biological Systems and Engineering Division, Lawrence Berkeley National Lab, Berkeley, California, USA.
  • Keasling JD; DOE Joint BioEnergy Institute, Emeryville, California, USA.
Nat Chem Biol ; 13(11): 1155-1157, 2017 Nov.
Article em En | MEDLINE | ID: mdl-28892091
Prodiginines, which are tripyrrole alkaloids displaying a wide array of bioactivities, occur as linear and cyclic congeners. Identification of an unclustered biosynthetic gene led to the discovery of the enzyme responsible for catalyzing the regiospecific C-H activation and cyclization of prodigiosin to cycloprodigiosin in Pseudoalteromonas rubra. This enzyme is related to alkylglycerol monooxygenase and unrelated to RedG, the Rieske oxygenase that produces cyclized prodiginines in Streptomyces, implying convergent evolution.
Assuntos

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Prodigiosina / Pseudoalteromonas / Oxigenases de Função Mista Idioma: En Revista: Nat Chem Biol Assunto da revista: BIOLOGIA / QUIMICA Ano de publicação: 2017 Tipo de documento: Article País de afiliação: Estados Unidos

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Prodigiosina / Pseudoalteromonas / Oxigenases de Função Mista Idioma: En Revista: Nat Chem Biol Assunto da revista: BIOLOGIA / QUIMICA Ano de publicação: 2017 Tipo de documento: Article País de afiliação: Estados Unidos