Conversion of reticuline into scoulerine by a cell free preparation from <i>Macleaya microcarpa</i> cell suspension cultures

Rink, Erika; Böhm, H.

doi:10.1016/0014-5793(75)80794-0

Cited by 53 publications

(24 citation statements)

References 7 publications

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“…[10] The enzyme is found in plants, mainly from the poppy family, where it plays a central role in the biosynthesis of benzophenantridine alkaloids. [11,12] Only recently, BBE from Eschscholzia californica (California poppy) could be expressed efficiently in Pichia pastoris [13] to give a sufficient quantity of the enzyme for crystallization and investigation of the mechanism. [10,14] Thus, BBE has been thoroughly investigated regarding its biochemical properties and catalytic mechanism, while its potential as a biocatalyst for preparative transformation of non-natural substrates has not been explored yet.…”

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confidence: 99%

Biocatalytic Enantioselective Oxidative CC Coupling by Aerobic CH Activation

et al. 2011

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confidence: 99%

Biocatalytic Enantioselective Oxidative CC Coupling by Aerobic CH Activation

et al. 2011

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“…Each of the 12 enzymes involved has been identified and partially characterized (12)(13)(14)(15)(16). Of particular interest in this pathway is the branch-point enzyme that catalyzes the formation of (S)-scoulerine from (S)-reticuline, the berberine bridge enzyme [(S)-reticuline:oxygen oxidoreductase (methylene-bridge-forming), EC 1.5.3.9] (17,18). The formation of the berberine bridge was demonstrated to arise by an oxidative cyclization of the N-methyl group of (S)-reticuline (19,20).…”

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Molecular cloning, expression, and induction of berberine bridge enzyme, an enzyme essential to the formation of benzophenanthridine alkaloids in the response of plants to pathogenic attack.

Dittrich

Kutchan

1991

Proc. Natl. Acad. Sci. U.S.A.

246

165

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The berberine bridge enzyme [(S)-reticuline: oxygen oxidoreductase (methylene-bridge-forming), EC 1.5.3.9] is a vesicular plant enzyme that catalyzes the formation of the berberine bridgehead carbon of (S)-scoulerine from the N-methyl carbon of (S)-reticuline in a specific, unparalleled reaction along the biosynthetic pathway that leads to benzophenanthridine alkaloids. Cytotoxic benzophenanthridine alkaloids are accumulated in certain species of Papaveraceae and Fumariaceae in response to pathogenic attack and, therefore, function as phytoalexins. The berberine bridge enzyme has been purified to homogeneity from elicited cell-suspension cultures of Eschscholtzia calafornica, and partial amino acid sequences have been determined. A cDNA, isolated from a Agtll cDNA bank of elicited E. calzfornica cell-suspension cultures, coded for an open reading frame of 538 amino acids. The first 22 amino acids constitute the putative signal peptide. The mature protein has a Mr of 57,352, excluding carbohydrate. The berberine bridge enzyme was heterologously expressed in a catalytically active form in Saccharomyces cerevisiae. Southern hybridization with genomic DNA suggests that there is only one gene for the enzyme in the E. californica genome. Hybridized RNA blots from elicited E. calafornica cell-suspension cultures revealed a rapid and transient increase in poly(A)+ RNA levels that preceded both the increase in enzyme activity and the accumulation of benzophenanthridine alkaloids, emphasizing the integral role of the berberine bridge enzyme in the plant response to pathogens.

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“…The berberine bridge enzyme ((S)-reticuline:oxygen oxidoreductase (methylene-bridge-forming), EC 1.5.3.9) transforms the N-methyl group of (S)-reticuline into the berberine bridge carbon, C-8, of (S)-scoulerine, thereby forming the protoberberine carbon skeleton (1,2). (S)-Scoulerine then serves as the biosynthetic precursor to a multitude of species-specific protopine, protoberberine and benzophenanthridine alkaloids (Fig.…”

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Characterization and Mechanism of the Berberine Bridge Enzyme, a Covalently Flavinylated Oxidase of Benzophenanthridine Alkaloid Biosynthesis in Plants

Kutchan¹,

Dittrich²

1995

Journal of Biological Chemistry

146

125

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The berberine bridge enzyme ((S)-reticuline:oxygen oxidoreductase (methylene-bridge-forming), EC 1.5.3.9) catalyzes the oxidative cyclization of the N-methyl moiety of (S)-reticuline into the berberine bridge carbon, C-8, of (S)-scoulerine. This is a reaction that has neither an equivalent in organic chemistry nor a parallel in nature. The uniqueness of this catalytic reaction prompted an in depth study that began with the isolation of the cDNA encoding the berberine bridge enzyme followed by the overexpression of this cDNA in insect cell culture. The heterologously expressed enzyme has herein been shown to contain covalently attached FAD in a molar ratio of cofactor to protein of 1:1.03. Sitedirected mutagenesis and laser desorption time-of-flight mass spectrometry suggest that the site of covalent attachment is at His-104. The holoenzyme exhibited absorbance maxima at 380 and 442 nm and a fluorescence emission maximum at 628 nm (310 nm excitation). Enzymic transformation of a series of (S)-reticuline derivatives modified with respect to the stereochemistry at C-1 or in the aromatic ring substitution suggests that ring closure proceeds in two steps: formation of the methylene iminium ion and subsequent ring closure via an ionic mechanism.

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Conversion of reticuline into scoulerine by a cell free preparation from Macleaya microcarpa cell suspension cultures

Cited by 53 publications

References 7 publications

Biocatalytic Enantioselective Oxidative CC Coupling by Aerobic CH Activation

Biocatalytic Enantioselective Oxidative CC Coupling by Aerobic CH Activation

Molecular cloning, expression, and induction of berberine bridge enzyme, an enzyme essential to the formation of benzophenanthridine alkaloids in the response of plants to pathogenic attack.

Characterization and Mechanism of the Berberine Bridge Enzyme, a Covalently Flavinylated Oxidase of Benzophenanthridine Alkaloid Biosynthesis in Plants

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