scholarly journals Enzymatic synthesis of natural (+)-aristolochene from a non-natural substrate

2016 ◽  
Vol 52 (97) ◽  
pp. 14027-14030 ◽  
Author(s):  
Juan A. Faraldos ◽  
Daniel J. Grundy ◽  
Oscar Cascon ◽  
Stefano Leoni ◽  
Marc W. van der Kamp ◽  
...  
Keyword(s):  
Natural Product ◽  
Enzymatic Synthesis ◽  
Penicillium Roqueforti ◽  
Natural Substrate ◽  
Aristolochene Synthase

Aristolochene synthase from Penicillium roqueforti converts 7-methylene-FDP, a substrate the enzyme never encounters in nature, to the natural product (+)-aristolochene.

Substrate specificity of fucosyl transferase III: An efficient synthesis of sialyl Lewisx-, sialyl Lewisa-derivatives and mimetics thereof

2000 ◽  
Vol 78 (6) ◽  
pp. 892-904 ◽  
Author(s):  
Beat Ernst ◽  
Bea Wagner ◽  
Gabi Baisch ◽  
Andreas Katopodis ◽  
Tammo Winkler ◽  
...  
Keyword(s):  
Substrate Specificity ◽  
Enzymatic Synthesis ◽  
Reaction Rates ◽  
Efficient Synthesis ◽  
Natural Substrate ◽  
Sialyl Lewisx ◽  
Sialyl Lewis ◽  
Sialyl Lewisa

Fucosyl transferase III (FucT III) has previously been characterized as the most general enzyme of the FucT family, as judged from its ability to catalyze the transfer of fucose to both Galβ(1-3)GlcNAc and Galβ(1-4)GlcNAc. In order to explore the synthetic potential of FucT III for the enzymatic synthesis of sialyl Lewisx and sialyl Lewisa derivatives, its substrate specificity has been probed using a number of natural substrate mimetics. A remarkable range of acceptor substrates was found when N-acetyl glucosamine was replaced by D-glucal, (R,R)-1,2-cyclohexanediol and (R,R)-butan-2,3-diol. Although the reaction rates were low compared to the reaction with the natural substrates, they proved to be sufficient for the synthesis of preparative amounts.Key words: fucosyl transferase III, sialyl Lewisa, sialyl Lewisx, carbohydrate mimetics.

scholarly journals Crystal Structure Determination of Aristolochene Synthase from the Blue Cheese Mold,Penicillium roqueforti*

2000 ◽  
Vol 275 (33) ◽  
pp. 25533-25539 ◽  
Author(s):  
Jonathan M. Caruthers ◽  
Ilgu Kang ◽  
Michael J. Rynkiewicz ◽  
David E. Cane ◽  
David W. Christianson
Keyword(s):  
Crystal Structure ◽  
Structure Determination ◽  
Crystal Structure Determination ◽  
Penicillium Roqueforti ◽  
Blue Cheese ◽  
Aristolochene Synthase

Chemo-enzymatic synthesis of the C15–C23 unit of Leptomycin B

2002 ◽  
Vol 80 (6) ◽  
pp. 571-576 ◽  
Author(s):  
Michael Scheck ◽  
Herbert Waldmann
Keyword(s):  
Asymmetric Synthesis ◽  
Natural Product ◽  
Building Block ◽  
Enzymatic Synthesis ◽  
Aldol Reaction ◽  
Natural Product Synthesis ◽  
Leptomycin B ◽  
Enzymatic Transformation

The asymmetric synthesis of the C15–C23 unit of Leptomycin B (LMB) is described. All four stereocenters of the C15–C23 unit were prepared from one building block exhibiting only one stereocenter. This building block was synthesized via either an enzymatic transformation or starting from a chiral reagent.Key words: Leptomycin, natural product synthesis, enzymatic transformation, Aldol reaction, Pseudomonas fluorescence lipase (PFL).

Stereochemistry of eudesmane cation formation during catalysis by aristolochene synthase from Penicillium roqueforti

2008 ◽  
Vol 6 (13) ◽  
pp. 2346 ◽  
Author(s):  
David J. Miller ◽  
Jiali Gao ◽  
Donald G. Truhlar ◽  
Neil J. Young ◽  
Veronica Gonzalez ◽  
...  
Keyword(s):  
Penicillium Roqueforti ◽  
Aristolochene Synthase

Synthetic studies toward inducamide C

2021 ◽  
Author(s):  
Ardalan A. Nabi ◽  
Lydia M. Scott ◽  
Daniel P. Furkert ◽  
Jonathan Sperry
Keyword(s):  
Natural Product ◽  
Structural Revision ◽  
Synthetic Studies

The rare benzoxazepine ring in the alkaloid inducamide C is unstable and prone to rearrangement, indicating that structural revision of the natural product may be necessary.

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