A bifunctional old yellow enzyme from Penicillium roqueforti is involved in ergot alkaloid biosynthesis

2017 ◽  
Vol 15 (38) ◽  
pp. 8059-8071 ◽  
Author(s):  
Nina Gerhards ◽  
Shu-Ming Li
Keyword(s):  
Ergot Alkaloid ◽  
Penicillium Roqueforti ◽  
Alkaloid Biosynthesis ◽  
Old Yellow Enzyme

Bifunctional FgaOx3Pr3catalyses the formation of festuclavine in the presence of EasG or FgaFS and enhances the activity of several chanoclavine-I dehydrogenases tremendously.

A Role for Old Yellow Enzyme in Ergot Alkaloid Biosynthesis

2010 ◽  
Vol 132 (6) ◽  
pp. 1776-1777 ◽  
Author(s):  
Johnathan Z. Cheng ◽  
Christine M. Coyle ◽  
Daniel G. Panaccione ◽  
Sarah E. O’Connor
Keyword(s):  
Ergot Alkaloid ◽  
Alkaloid Biosynthesis ◽  
Old Yellow Enzyme

scholarly journals Structure of anAspergillus fumigatusold yellow enzyme (EasA) involved in ergot alkaloid biosynthesis

2014 ◽  
Vol 70 (10) ◽  
pp. 1328-1332 ◽  
Author(s):  
Annemarie S. Chilton ◽  
Ashley L. Ellis ◽  
Audrey L. Lamb
Keyword(s):  
Crystal Structure ◽  
Amino Acids ◽  
Aspergillus Fumigatus ◽  
Ergot Alkaloid ◽  
Active Site ◽  
Self Regulation ◽  
Unsaturated Aldehyde ◽  
Asymmetric Unit ◽  
Alkaloid Biosynthesis ◽  
Old Yellow Enzyme

TheAspergillus fumigatusold yellow enzyme (OYE) EasA reduces chanoclavine-I aldehyde to dihydrochanoclavine aldehyde and works in conjunction with festuclavine synthase at the branchpoint for ergot alkaloid pathways. The crystal structure of the FMN-loaded EasA was determined to 1.8 Å resolution. The active-site amino acids of OYE are conserved, supporting a similar mechanism for reduction of the α/β-unsaturated aldehyde. The C-terminal tail of one monomer packs into the active site of a monomer in the next asymmetric unit, which is most likely to be a crystallization artifact and not a mechanism of self-regulation.

Probing ergot alkaloid biosynthesis: identification of advanced intermediates along the biosynthetic pathway

1988 ◽  
Vol 110 (6) ◽  
pp. 1970-1971 ◽  
Author(s):  
Alan P. Kozikowski ◽  
Jiang Ping. Wu ◽  
Masaaki. Shibuya ◽  
Heinz G. Floss
Keyword(s):  
Ergot Alkaloid ◽  
Biosynthetic Pathway ◽  
Alkaloid Biosynthesis

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

Sign in / Sign up

Export Citation Format

Share Document