scholarly journals Correction to Multisite Prenylation of 4-Substituted Tryptophans by Dimethylallyltryptophan Synthase

2013 ◽  
Vol 135 (29) ◽  
pp. 10879-10879 ◽  
Author(s):  
Jeffrey D. Rudolf ◽  
Hong Wang ◽  
C. Dale Poulter
Keyword(s):  
Dimethylallyltryptophan Synthase

Overproduction, purification and characterization of FtmPT1, a brevianamide F prenyltransferase from Aspergillus fumigatus

Microbiology ◽  
2005 ◽  
Vol 151 (7) ◽  
pp. 2199-2207 ◽  
Author(s):  
Alexander Grundmann ◽  
Shu-Ming Li
Keyword(s):  
Aspergillus Fumigatus ◽  
Enzymic Activity ◽  
Divalent Metal Ions ◽  
Purification And Characterization ◽  
Turnover Number ◽  
Dimethylallyl Diphosphate ◽  
Dimethylallyltryptophan Synthase ◽  
Aromatic Substrates ◽  
Prenyl Diphosphate

A putative prenyltransferase gene, ftmPT1, was identified in the genome sequence of Aspergillus fumigatus. ftmPT1 was cloned and expressed in Escherichia coli, and the protein FtmPT1 was purified to near homogeneity and characterized biochemically. This enzyme was found to catalyse the prenylation of cyclo-l-trp-l-Pro (brevianamide F) at the C-2 position of the indole nucleus. FtmPT1 is a soluble monomeric protein, which does not contain the usual prenyl diphosphate binding site (N/D)DXXD found in most prenyltransferases, and which does not require divalent metal ions for its enzymic activity. K m values for brevianamide F and dimethylallyl diphosphate were determined as 55 and 74 μM, respectively. The turnover number was 5·57 s−1. FtmPT1 showed a high substrate specificity towards dimethylallyl diphosphate, but accepted different tryptophan-containing cyclic dipeptides. Together with dimethylallyltryptophan synthase of ergot alkaloid biosynthesis, FtmPT1 belongs to a new group of prenyltransferases with aromatic substrates.

scholarly journals Erratum to: Silencing of a second dimethylallyltryptophan synthase of Penicillium roqueforti reveals a novel clavine alkaloid gene cluster

2017 ◽  
Vol 101 (20) ◽  
pp. 7767-7768
Author(s):  
Ángeles Fernández-Bodega ◽  
Rubén Álvarez-Álvarez ◽  
Paloma Liras ◽  
Juan F. Martín
Keyword(s):  
Gene Cluster ◽  
Penicillium Roqueforti ◽  
Dimethylallyltryptophan Synthase

scholarly journals Towards the elimination of ergot alkaloid biosynthesis genes in Neotyphodium Coenophialum

2007 ◽  
Vol 13 ◽  
pp. 477-479
Author(s):  
S. Florea ◽  
C. Machado ◽  
D. Zhang ◽  
D.G. Panaccione ◽  
C.L. Schardl
Keyword(s):  
Tall Fescue ◽  
Ergot Alkaloid ◽  
Festuca Arundinacea ◽  
Ergot Alkaloids ◽  
Loxp Site ◽  
Alkaloid Biosynthesis ◽  
Neotyphodium Coenophialum ◽  
Type Locus ◽  
Dimethylallyltryptophan Synthase ◽  
Recombination System

Neotyphodium coenophialum strain e19 from tall fescue cv. Kentucky 31 carries dmaW1 and dmaW2, two gene homologues that encode dimethylallyltryptophan synthase, the enzyme for the first step in ergot-alkaloid biosynthesis. In our effort to disrupt both homologues and ultimately obtain marker-free mutants, we are using a marker-exchange strategy employing the Cre/ loxP site-specific recombination system. Of 1522 transformants obtained and screened, three were likely dmaW2 disruptants because they gave no PCR product from the wild-type locus, but yielded the larger PCR fragment from the disruption construct. The putative dmaW2-knockouts were also transformed with pKAES186, a plasmid with a cassette containing the cre and ble genes in between loxP sequences. The transformants obtained were screened for the presence of hph, cre and ble genes. The preliminary results indicate a loop-out of the hph gene. The transformants inoculated into endophyte-free tall fescue preserved their compatibility with the plant. The fungus grown from these plants will be further analysed for the presence of hph, cre and ble genes. Keywords: Cre/LoxP, dimethylallyltryptophan synthase, dmaW, Epichloë, ergot alkaloids, Festuca arundinacea, gene knockouts, Lolium arundinaceum, Neotyphodium coenophialum, tall fescue

gem-Diprenylation of Acylphloroglucinols by a Fungal Prenyltransferase of the Dimethylallyltryptophan Synthase Superfamily

2016 ◽  
Vol 19 (2) ◽  
pp. 388-391 ◽  
Author(s):  
Kang Zhou ◽  
Carsten Wunsch ◽  
Jungui Dai ◽  
Shu-Ming Li
Keyword(s):  
Dimethylallyltryptophan Synthase
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