Elicitor induced : Caffeoyl-CoA 3-O-methyltransferase from carrot cell suspension cultures

Kühnl, Thomas; Koch, Ulrich; Heller, Werner; Wellmann, Eckard

doi:10.1016/0168-9452(89)90039-3

Cited by 59 publications

(33 citation statements)

References 14 publications

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“…If shikimate esters are described as transient intermediates, quinate derivatives such as chlorogenic acid commonly accumulate in some plant species and are alternatively described as growth regulators, disease resistance factors, antioxidants, and compounds affecting organoleptic quality of fruits (36,38,54,55 This leads to another interesting question concerning the branching of the pathway downstream of C3ЈH. Our data and previous reports (17,51) seem to indicate that the shikimate and quinate esters are not substrates of CCoAOMTs. This has to be confirmed in other plant species and with other recombinant CCoAOMTs, but it seems that the caffeate ester(s) have to be converted back to CoA esters for further methylation.…”

Section: Cyp98a3 a 3ј-hydroxylase Of P-coumaroyl Esters In Arabidopsismentioning

confidence: 47%

“…It was, however, very early suggested by the work of Ulbricht and Zenk (34), who demonstrated the existence of a p-hydroxycinnamoyl-CoA:shikimate p-hydroxycinnamoyltransferase in a broad range of plant species that never accumulate shikimate esters. This work was further supported by the biochemical characterization of a P450-dependent 3Ј-hydroxylation of the shikimate and quinate esters of p-coumaric acid in microsomal fractions of parsley and carrot cell cultures (7,9) and by the characterization of caffeoyl-CoA 3-O-methyltransferase activity in the soluble fraction of the same carrot cell cultures (51). Further investigations in this direction were never pursued, however.…”

Section: Cyp98a3 a 3ј-hydroxylase Of P-coumaroyl Esters In Arabidopsismentioning

confidence: 75%

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CYP98A3 from Arabidopsis thaliana Is a 3′-Hydroxylase of Phenolic Esters, a Missing Link in the Phenylpropanoid Pathway

Schoch

Goepfert

Morant

et al. 2001

Journal of Biological Chemistry

396

370

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The 4-and 5-hydroxylations of phenolic compounds in plants are catalyzed by cytochrome P450 enzymes. The 3-hydroxylation step leading to the formation of caffeic acid from p-coumaric acid remained elusive, however, alternatively described as a phenol oxidase, a dioxygenase, or a P450 enzyme, with no decisive evidence for the involvement of any in the reaction in planta. In this study, we show that the gene encoding CYP98A3, which was the best possible P450 candidate for a 3-hydroxylase in the Arabidopsis genome, is highly expressed in inflorescence stems and wounded tissues. Recombinant CYP98A3 expressed in yeast did not metabolize free pcoumaric acid or its glucose or CoA esters, p-coumaraldehyde, or p-coumaryl alcohol, but very actively converted the 5-O-shikimate and 5-O-D-quinate esters of trans-p-coumaric acid into the corresponding caffeic acid conjugates. The shikimate ester was converted four times faster than the quinate derivative. Antibodies directed against recombinant CYP98A3 specifically revealed differentiating vascular tissues in stem and root. Taken together, these data show that CYP98A3 catalyzes the synthesis of chlorogenic acid and very likely also the 3-hydroxylation of lignin monomers. This hydroxylation occurs on depsides, the function of which was so far not understood, revealing an additional and unexpected level of networking in lignin biosynthesis.Systematic genome sequencing is revealing a large number of orphan genes and their phylogenetic relatedness to genes with characterized function. EST 1 sequences, on the other hand, are providing preliminary information on levels, patterns of expression, and conservation of genes among species. Taken together, such information can be exploited as a clue to gene function and to track down missing steps in important pathways.The sequencing of the whole genome of Arabidopsis thaliana has revealed 273 cytochrome P450 genes distributed into 45 families and subfamilies (drnelson.utmem.edu/CytochromeP450. html, www.biobase.dk/P450/). P450 proteins thus form the largest superfamily of enzymes involved in plant metabolism, but the function of 80% of these enzymes is still unknown. Our attention was first drawn to the CYP98 family by its phylogeny and structure. An analysis of P450 phylogeny in A. thaliana (Fig. 1) shows that the CYP98 family is most closely related to CYP73A5, coding for the cinnamic-acid 4-hydroxylase, the second enzyme and first P450 in the phenylpropanoid pathway (1). CYP73A5 and the CYP98 family seem to have evolved from the same ancestor as CYP79 enzymes, some of which also, in common with CYP73A5, use aromatic substrates derived from the shikimate pathway (2, 3). It was thus tempting to speculate that the substrate of CYP98 enzymes was derived from aromatic amino acids as well. The Arabidopsis CYP98 family is formed by only three genes. CYP98A3 is present in single copy; CYP98A8 and CYP98A9 are 69% identical to one another and only 52% identical to CYP98A3. All P450 genes in the phenylpropanoid pathway (CYP73A5, CYP84A1, and CYP...

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Section: Cyp98a3 a 3ј-hydroxylase Of P-coumaroyl Esters In Arabidopsismentioning

confidence: 47%

Section: Cyp98a3 a 3ј-hydroxylase Of P-coumaroyl Esters In Arabidopsismentioning

confidence: 75%

CYP98A3 from Arabidopsis thaliana Is a 3′-Hydroxylase of Phenolic Esters, a Missing Link in the Phenylpropanoid Pathway

Schoch

Goepfert

Morant

et al. 2001

Journal of Biological Chemistry

396

370

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“…In the phenylpropanoid biosynthetic pathway, another OMT, S-adenosyl-L-methionine:transcaffeoyl-coenzyme A 3-Omethyltransferase (CCoAOMT) was found in parsley and carrot cell suspension cultures (Matern et al, 1988;Kühnl et al, 1989;Pakusch et al, 1989). The enzyme activity rapidly increases in response to funga1 elicitor treatment in both parsley and carrot cell suspension cultures (Matern et al, 1988;Kühnl et al, 1989;Pakusch et al, 1989).…”

Section: Introductionmentioning

confidence: 99%

An alternative methylation pathway in lignin biosynthesis in Zinnia.

et al. 1994

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“…However, this hypothesis was largely ignored probably due to the early demonstration that COMT used the acid forms of hydroxycinnamates as substrates. An OMT that uses CoA ester forms of hydroxycinnamates as substrates was first detected in parsley and carrot (Kü hnl et al, 1989;Pakusch et al, 1989;Fig. 1).…”

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confidence: 99%

Essential Role of Caffeoyl Coenzyme A O-Methyltransferase in Lignin Biosynthesis in Woody Poplar Plants

et al. 2000

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Caffeoyl coenzyme A O-methyltransferase (CCoAOMT) has recently been shown to participate in lignin biosynthesis in herbacious tobacco plants. Here, we demonstrate that CCoAOMT is essential in lignin biosynthesis in woody poplar (Populus tremula ϫ Populus alba) plants. In poplar stems, CCoAOMT was found to be expressed in all lignifying cells including vessel elements and fibers as well as in xylem ray parenchyma cells. Repression of CCoAOMT expression by the antisense approach in transgenic poplar plants caused a significant decrease in total lignin content as detected by both Klason lignin assay and Fourier-transform infrared spectroscopy. The reduction in lignin content was the result of a decrease in both guaiacyl and syringyl lignins as determined by in-source pyrolysis mass spectrometry. Fourier-transform infrared spectroscopy indicated that the reduction in lignin content resulted in a less condensed and less cross-linked lignin structure in wood. Repression of CCoAOMT expression also led to coloration of wood and an elevation of wall-bound p-hydroxybenzoic acid. Taken together, these results indicate that CCoAOMT plays a dominant role in the methylation of the 3-hydroxyl group of caffeoyl CoA, and the CCoAOMT-mediated methylation reaction is essential to channel substrates for 5-methoxylation of hydroxycinnamates. They also suggest that antisense repression of CCoAOMT is an efficient means for genetic engineering of trees with low lignin content.

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Elicitor induced : Caffeoyl-CoA 3-O-methyltransferase from carrot cell suspension cultures

Cited by 59 publications

References 14 publications

CYP98A3 from Arabidopsis thaliana Is a 3′-Hydroxylase of Phenolic Esters, a Missing Link in the Phenylpropanoid Pathway

CYP98A3 from Arabidopsis thaliana Is a 3′-Hydroxylase of Phenolic Esters, a Missing Link in the Phenylpropanoid Pathway

An alternative methylation pathway in lignin biosynthesis in Zinnia.

Essential Role of Caffeoyl Coenzyme A O-Methyltransferase in Lignin Biosynthesis in Woody Poplar Plants

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