Literature DB >> 18677738

Two lysine residues are responsible for the enzymatic activities of indole prenyltransferases from fungi.

Edyta Stec1, Nicola Steffan, Anika Kremer, Huixi Zou, Xiaodong Zheng, Shu-Ming Li.   

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Year:  2008        PMID： 18677738     DOI： 10.1002/cbic.200800237

Source DB:  PubMed          Journal:  Chembiochem        ISSN： 1439-4227            Impact factor:   3.164


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  4 in total

1.  Site-directed mutagenesis switching a dimethylallyl tryptophan synthase to a specific tyrosine C3-prenylating enzyme.

Authors:  Aili Fan; Georg Zocher; Edyta Stec; Thilo Stehle; Shu-Ming Li
Journal:  J Biol Chem       Date:  2014-12-04       Impact factor: 5.157

2.  Functional characterization of the cyclomarin/cyclomarazine prenyltransferase CymD directs the biosynthesis of unnatural cyclic peptides.

Authors:  Andrew W Schultz; Chad A Lewis; Michael R Luzung; Phil S Baran; Bradley S Moore
Journal:  J Nat Prod       Date:  2010-03-26       Impact factor: 4.050

3.  The structure of dimethylallyl tryptophan synthase reveals a common architecture of aromatic prenyltransferases in fungi and bacteria.

Authors:  Ute Metzger; Christoph Schall; Georg Zocher; Inge Unsöld; Edyta Stec; Shu-Ming Li; Lutz Heide; Thilo Stehle
Journal:  Proc Natl Acad Sci U S A       Date:  2009-08-12       Impact factor: 11.205

4.  Characterization of cyclo-acetoacetyl-L-tryptophan dimethylallyltransferase in cyclopiazonic acid biosynthesis: substrate promiscuity and site directed mutagenesis studies.

Authors:  Xinyu Liu; Christopher T Walsh
Journal:  Biochemistry       Date:  2009-11-24       Impact factor: 3.162
  4 in total

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