Literature DB >> 16408001

Relaxed specificity in aromatic prenyltransferases.

Patrice Koehl.   

Abstract

Prenylation represent a critical step in the biosynthesis of many natural products, A new study reveals how aromatic prenyltransferase enzymes tolerate diverse aromatic polyketides while still controlling the length of prenyl side chains.

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Year:  2005        PMID： 16408001     DOI： 10.1038/nchembio0705-71

Source DB:  PubMed          Journal:  Nat Chem Biol        ISSN： 1552-4450            Impact factor:   15.040


  3 in total

1.  A new group of aromatic prenyltransferases in fungi, catalyzing a 2,7-dihydroxynaphthalene 3-dimethylallyl-transferase reaction.

Authors:  Elisa Haug-Schifferdecker; Deniz Arican; Reinhard Brückner; Lutz Heide
Journal:  J Biol Chem       Date:  2010-03-29       Impact factor: 5.157

Review 2.  Biosynthesis of Nature-Inspired Unnatural Cannabinoids.

Authors:  Kevin J H Lim; Yan Ping Lim; Yossa D Hartono; Maybelle K Go; Hao Fan; Wen Shan Yew
Journal:  Molecules       Date:  2021-05-14       Impact factor: 4.411

3.  A soluble, magnesium-independent prenyltransferase catalyzes reverse and regular C-prenylations and O-prenylations of aromatic substrates.

Authors:  Yvonne Haagen; Inge Unsöld; Lucia Westrich; Bertolt Gust; Stéphane B Richard; Joseph P Noel; Lutz Heide
Journal:  FEBS Lett       Date:  2007-05-22       Impact factor: 4.124
  3 in total

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