scholarly journals Biosynthesis of a Tricyclo[6.2.2.0 2,7 ]dodecane System by a Berberine Bridge Enzyme‐Like Aldolase

2019 ◽  
Vol 25 (66) ◽  
pp. 15062-15066 ◽  
Author(s):  
Hang Li ◽  
Jinyu Hu ◽  
Haochen Wei ◽  
Peter S. Solomon ◽  
Keith A. Stubbs ◽  
...  
Keyword(s):  
Berberine Bridge Enzyme

scholarly journals The single berberine bridge enzyme homolog ofPhyscomitrella patensis a cellobiose oxidase

FEBS Journal ◽  
2018 ◽  
Vol 285 (10) ◽  
pp. 1923-1943 ◽  
Author(s):  
Marina Toplak ◽  
Gertrud Wiedemann ◽  
Jelena Ulićević ◽  
Bastian Daniel ◽  
Sebastian N. W. Hoernstein ◽  
...  
Keyword(s):  
Berberine Bridge Enzyme

scholarly journals Isotope Effects Suggest a Stepwise Mechanism for Berberine Bridge Enzyme

Biochemistry ◽  
2012 ◽  
Vol 51 (37) ◽  
pp. 7342-7347 ◽  
Author(s):  
Helena M. Gaweska ◽  
Kenneth M. Roberts ◽  
Paul F. Fitzpatrick
Keyword(s):  
Isotope Effects ◽  
Stepwise Mechanism ◽  
Berberine Bridge Enzyme

scholarly journals Biochemical Evidence That Berberine Bridge Enzyme Belongs to a Novel Family of Flavoproteins Containing a Bi-covalently Attached FAD Cofactor

2006 ◽  
Vol 281 (30) ◽  
pp. 21276-21285 ◽  
Author(s):  
Andreas Winkler ◽  
Franz Hartner ◽  
Toni M. Kutchan ◽  
Anton Glieder ◽  
Peter Macheroux
Keyword(s):  
Biochemical Evidence ◽  
Berberine Bridge Enzyme

Knockdown of berberine bridge enzyme by RNAi accumulates (S)-reticuline and activates a silent pathway in cultured California poppy cells

2006 ◽  
Vol 16 (3) ◽  
pp. 363-375 ◽  
Author(s):  
Nanae Fujii ◽  
Takayuki Inui ◽  
Kinuko Iwasa ◽  
Takashi Morishige ◽  
Fumihiko Sato
Keyword(s):  
California Poppy ◽  
Berberine Bridge Enzyme

scholarly journals An Arabidopsis berberine bridge enzyme‐like protein specifically oxidizes cellulose oligomers and plays a role in immunity

2019 ◽  
Vol 98 (3) ◽  
pp. 540-554 ◽  
Author(s):  
Federica Locci ◽  
Manuel Benedetti ◽  
Daniela Pontiggia ◽  
Matteo Citterico ◽  
Claudio Caprari ◽  
...  
Keyword(s):  
Berberine Bridge Enzyme

scholarly journals Cannabinoid Biosynthesis using Noncanonical Cannabinoid Synthases

2020 ◽  
Author(s):  
Maybelle K. Go ◽  
Kevin Jie Han Lim ◽  
Wen Shan Yew
Keyword(s):  
Heterologous Expression ◽  
Oxidative Cyclization ◽  
First Report ◽  
Enzyme Superfamily ◽  
Berberine Bridge Enzyme

We have found enzymes from the berberine-bridge enzyme (BBE) superfamily (IPR012951) that catalyze the oxidative cyclization of the monoterpene moiety in cannabigerolic acid (CBGA) to form cannabielsoic acid B (CBSA). The enzymes are from a variety of organisms and are previously uncharacterized. This is the first report that describes enzymes that did not originate from the Cannabis plant that catalyze the production of cannabinoids. Out of 72 homologues chosen from the enzyme superfamily, six orthologues were shown to accept CBGA as a substrate and catalyze the biosynthesis of CBSA. The six enzymes discovered in this study are the first report of heterologous expression of BBEs that did not originate from the Cannabis plant that catalyze the production of cannabinoids using CBGA as substrate. This study details a new avenue for discovering and producing natural and unnatural cannabinoids.

scholarly journals Oxidative cyclization of N-methyl-dopa by a fungal flavoenzyme of the amine oxidase family

2018 ◽  
Vol 293 (44) ◽  
pp. 17021-17032
Author(s):  
Majd Lahham ◽  
Tea Pavkov-Keller ◽  
Michael Fuchs ◽  
Johannes Niederhauser ◽  
Gabriel Chalhoub ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Amine Oxidase ◽  
Oxidative Cyclization ◽  
Ring Closure ◽  
Hydroxyl Group ◽  
Binding Modes ◽  
Recombinant Production ◽  
Methyl Dopa ◽  
Berberine Bridge Enzyme ◽  
Ring Structures

Flavin-dependent enzymes catalyze many oxidations, including formation of ring structures in natural products. The gene cluster for biosynthesis of fumisoquins, secondary metabolites structurally related to isoquinolines, in the filamentous fungus Aspergillus fumigatus harbors a gene that encodes a flavoprotein of the amine oxidase family, termed fsqB (fumisoquin biosynthesis gene B). This enzyme catalyzes an oxidative ring closure reaction that leads to the formation of isoquinoline products. This reaction is reminiscent of the oxidative cyclization reported for berberine bridge enzyme and tetrahydrocannabinol synthase. Despite these similarities, amine oxidases and berberine bridge enzyme–like enzymes possess distinct structural properties, prompting us to investigate the structure–function relationships of FsqB. Here, we report the recombinant production and purification of FsqB, elucidation of its crystal structure, and kinetic analysis employing five putative substrates. The crystal structure at 2.6 Å resolution revealed that FsqB is a member of the amine oxidase family with a covalently bound FAD cofactor. N-methyl-dopa was the best substrate for FsqB and was completely converted to the cyclic isoquinoline product. The absence of the meta-hydroxyl group, as e.g. in l-N-methyl-tyrosine, resulted in a 25-fold lower rate of reduction and the formation of the demethylated product l-tyrosine, instead of a cyclic product. Surprisingly, FsqB did not accept the d-stereoisomer of N-methyltyrosine, in contrast to N-methyl-dopa, for which both stereoisomers were oxidized with similar rates. On the basis of the crystal structure and docking calculations, we postulate a substrate-dependent population of distinct binding modes that rationalizes stereospecific oxidation in the FsqB active site.

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