Δ 5 -3β-Hydroxysteroid dehydrogenase from Digitalis lanata Ehrh. - a multifunctional enzyme in steroid metabolism?

Finsterbusch, A.; Lindemann, Peter; Grimm, Rudolf; Eckerskorn, Christoph; Luckner, Martin

doi:10.1007/s004250050751

Cited by 58 publications

(52 citation statements)

References 38 publications

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“…AF097651; Brosché and Strid, 1999); D 5 -3b-hydroxysteroid dehydrogenase from Digitalis lanata (48% identity, 61% similarity; accession no. Q93Y47; Finsterbusch et al, 1999); secoisolariciresinol dehydrogenase from Forsythia x intermedia (43% identity, 61% similarity; accession no. AF352735) and Podophyllum peltatum (41% identity, 58% similarity; accession no.…”

Section: Sequence Analysismentioning

confidence: 99%

Monoterpene Metabolism. Cloning, Expression, and Characterization of (−)-Isopiperitenol/(−)-Carveol Dehydrogenase of Peppermint and Spearmint

2005

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The essential oils of peppermint (Mentha x piperita) and spearmint (Mentha spicata) are distinguished by the oxygenation position on the p-menthane ring of the constitutive monoterpenes that is conferred by two regiospecific cytochrome P450 limonene-3-and limonene-6-hydroxylases. Following hydroxylation of limonene, an apparently similar dehydrogenase oxidizes (2)-trans-isopiperitenol to (2)-isopiperitenone in peppermint and (2)-trans-carveol to (2)-carvone in spearmint. Random sequencing of a peppermint oil gland secretory cell cDNA library revealed a large number of clones that specified redox-type enzymes, including dehydrogenases. Full-length dehydrogenase clones were screened by functional expression in Escherichia coli using a recently developed in situ assay. A single full-length acquisition encoding (2)-trans-isopiperitenol dehydrogenase (ISPD) was isolated. The (2)-ISPD cDNA has an open reading frame of 795 bp that encodes a 265-residue enzyme with a calculated molecular mass of 27,191. Nondegenerate primers were designed based on the (2)-trans-ISPD cDNA sequence and employed to screen a spearmint oil gland secretory cell cDNA library from which a 5#-truncated cDNA encoding the spearmint homolog, (2)-trans-carveol-dehydrogenase, was isolated. Reverse transcription-PCR amplification and RACE were used to acquire the remaining 5#-sequence from RNA isolated from oil gland secretory cells of spearmint leaf. The fulllength spearmint dehydrogenase shares .99% amino acid identity with its peppermint homolog and both dehydrogenases are capable of utilizing (2)-trans-isopiperitenol and (2)-trans-carveol. These isopiperitenol/carveol dehydrogenases are members of the short-chain dehydrogenase/reductase superfamily and are related to other plant short-chain dehydrogenases/ reductases involved in secondary metabolism (lignan biosynthesis), stress responses, and phytosteroid biosynthesis, but they are quite dissimilar (approximately 13% identity) to the monoterpene reductases of mint involved in (2)-menthol biosynthesis. The isolation of the genes specifying redox enzymes of monoterpene biosynthesis in mint indicates that these genes arose from different ancestors and not by simple duplication and differentiation of a common progenitor, as might have been anticipated based on the common reaction chemistry and structural similarity of the substrate monoterpenes.Monoterpenes, the C 10 members of the terpenoid family of secondary metabolites, are largely responsible for the fragrance and flavor characteristics of plants and are well known as components of plant essential oils (Parry, 1969). The essential oils of both peppermint (Mentha x piperita), a sterile cross between Mentha spicata and Mentha aquatica (Murray et al., 1972;Harley and Brighton, 1977), and spearmint (Mentha spicata) consist primarily of monoterpenes (Lawrence, 1981) that are distinguished by the position of oxygenation on the p-menthane ring conferred by two distinct regiospecific cytochrome P450 limonene hydroxylases (Fig. 1). Thus, following cycliz...

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Section: Sequence Analysismentioning

confidence: 99%

Monoterpene Metabolism. Cloning, Expression, and Characterization of (−)-Isopiperitenol/(−)-Carveol Dehydrogenase of Peppermint and Spearmint

2005

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“…This protein contains 3␤-HSD and NmrA components. 3␤-HSD has been implicated in the biosynthesis of the steroid cardenolide in foxglove (Digitalis lanata) (69) and has been detected in potato and tobacco, suggesting a role in general steroid metabolism (70). In a proteomics survey of Panax ginseng, the abundance of 3␤-HSD increased in response to light and was linked to the biosynthesis of steroidal saponins (71).…”

Section: Lc-ms/ms Using Public and Opium Poppy-specific Databases-mentioning

confidence: 99%

Plant Defense Responses in Opium Poppy Cell Cultures Revealed by Liquid Chromatography-Tandem Mass Spectrometry Proteomics

Zulak

Khan

Alcantara

et al. 2009

Molecular & Cellular Proteomics

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“…The highest similarities were seen with sequences from other plants (Scherbak et al, 2009): (2)-isopiperitenol dehydrogenase from Mentha species (similarity of 55%; Ringer et al, 2005), D 5 -3b-hydroxysteroid dehydrogenase (HSD; EC 1.1.1.145) from Digitalis lanata (49%; Finsterbusch et al, 1999), and secoisolariciresinol dehydrogenase from Podophyllum peltatum (46%; Xia et al, 2001). The threedimensional structure of the Podophyllum protein has been solved (Youn et al, 2005), while the Mentha protein is the polypeptide with the highest similarity to the pea SADs for which an enzymatic function is known.…”

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confidence: 78%

The Pea SAD Short-Chain Dehydrogenase/Reductase: Quinone Reduction, Tissue Distribution, and Heterologous Expression

et al. 2011

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The pea (Pisum sativum) tetrameric short-chain alcohol dehydrogenase-like protein (SAD) family consists of at least three highly similar members (SAD-A, -B, and -C). According to mRNA data, environmental stimuli induce SAD expression. The aim of this study was to characterize the SAD proteins by examining their catalytic function, distribution in pea, and induction in different tissues. In enzyme activity assays using a range of potential substrates, the SAD-C enzyme was shown to reduce one-or two-ring-membered quinones lacking long hydrophobic hydrocarbon tails. Immunological assays using a specific antiserum against the protein demonstrated that different tissues and cell types contain small amounts of SAD protein that was predominantly located within epidermal or subepidermal cells and around vascular tissue. Particularly high local concentrations were observed in the protoderm of the seed cotyledonary axis. Two bow-shaped rows of cells in the ovary and the placental surface facing the ovule also exhibited considerable SAD staining. Ultraviolet-B irradiation led to increased staining in epidermal and subepidermal cells of leaves and stems. The different localization patterns of SAD suggest functions both in development and in responses to environmental stimuli. Finally, the pea SAD-C promoter was shown to confer heterologous wound-induced expression in Arabidopsis (Arabidopsis thaliana), which confirmed that the inducibility of its expression is regulated at the transcriptional level.

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Δ 5 -3β-Hydroxysteroid dehydrogenase from Digitalis lanata Ehrh. - a multifunctional enzyme in steroid metabolism?

Cited by 58 publications

References 38 publications

Monoterpene Metabolism. Cloning, Expression, and Characterization of (−)-Isopiperitenol/(−)-Carveol Dehydrogenase of Peppermint and Spearmint

Monoterpene Metabolism. Cloning, Expression, and Characterization of (−)-Isopiperitenol/(−)-Carveol Dehydrogenase of Peppermint and Spearmint

Plant Defense Responses in Opium Poppy Cell Cultures Revealed by Liquid Chromatography-Tandem Mass Spectrometry Proteomics

The Pea SAD Short-Chain Dehydrogenase/Reductase: Quinone Reduction, Tissue Distribution, and Heterologous Expression

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