Cytochrome P450s in Lignin Biosynthesis

Alber, A.; Ehlting, Jürgen

doi:10.1016/b978-0-12-416023-1.00004-5

Cited by 15 publications

(11 citation statements)

References 111 publications

(137 reference statements)

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“…The first enzyme, phenylalanine ammonia-lyase (PAL; E.C. 4.3.1.5), eliminates ammonia and leads to t-cinnamic acid which is hydroxylated in position 4 to 4-coumaric acid by cinnamic acid 4-hydroxylase (C4H), the probably best investigated cytochrome P450 monooxygenase in plants (Alber and Ehlting 2012). Especially in monocots an ammonia-lyase accepting L-tyrosine is found which directly leads to 4-coumaric acid (Young et al 1966).…”

Section: Biosynthesis Of Hydroxycinnamoyl Unitsmentioning

confidence: 99%

Hydroxycinnamoyltransferases in plant metabolism

Petersen

2015

Phytochem Rev

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Hydroxycinnamoyltransferases are enzymes transferring hydroxycinnamoyl units like cinnamoyl, 4-coumaroyl, caffeoyl, feruloyl and sinapoyl moieties from an activating residue such as coenzyme A or glucose or activated as hydroxycinnamoyl ester (e.g. chlorogenate) to an acceptor molecule, most commonly to an OH or NH 2 group as ester or amide. The hydroxycinnamoyl groups play either a ''decorating'' role or are building blocks of more complex structures. Proteins catalysing hydroxycinnamoyl transfer have been known for many decades and are nowadays investigated on molecular and structural levels. At least four different protein families give rise to enzymes with hydroxycinnamoyltransferase activity: serine carboxypeptidase-like proteins, tyramine hydroxycinnamoyltransferase-like enzymes, BAHD acyltransferases and GDSL-lipase/esterase-like enzymes. Interestingly, the same or very similar products can be formed by enzymes from different enzyme classes and using differently activated hydroxycinnamoyl units. This review will summarise the current literature data on the features of hydroxycinnamoyltransferases from the four different enzyme groups. Keywords BAHD acyltransferase Á GDSL lipase/esterase-like acyltransferase Á Phenolic metabolism Á Serine carboxypeptidase-like acyltransferase Á THT-like hydroxycinnamoyltransferase Abbreviations HCT Hydroxycinnamoyltransferase HQT Hydroxycinnamoyl-CoA:quinate hydroxycinnamoyltransferase HST Hydroxycinnamoyl-CoA:shikimate hydroxycinnamoyltransferase SCPL Serine caryboxypeptidase-like THT Tyramine hydroxycinnamoyltransferase Hydroxycinnamic acid moieties in plant secondary products (Hydroxy)cinnamoyl units such as cinnamic, 4-coumaric, caffeic, ferulic and sinapic acids and their reduced derivatives (aldehydes, alcohols) are ubiquitous building blocks in plant secondary metabolites. In many cases, the (hydroxy)cinnamoyl unit is an essential structural feature, in other cases it is a ''decorating'' part of the molecule (Petersen et al. 2010 and literature cited therein). Substituted hydroxycinnamyl alcohols (4-coumaryl, coniferyl = guajacyl, sinapyl = syringyl units) are the basis for the M. Petersen (&)

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Section: Biosynthesis Of Hydroxycinnamoyl Unitsmentioning

confidence: 99%

Hydroxycinnamoyltransferases in plant metabolism

Petersen

2015

Phytochem Rev

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“…The present work indicated that there are at least two C4Hs in C. acuminata and CaC4H2 was proven to catalyze the regioselective para-hydroxylation of trans-cinnamic acid to form p-coumaric acid. The latter one is the biosynthetic intermediate leading to the phenylpropanoid biopolymers (Schalk et al 1999;Ehlting et al 2006;Vogt 2010;Alber and Ehlting 2012). As one of the most widely distributed phenolic acids in plants, pcoumaric acid was an important natural product with significant biological activities and it has been shown to have beneficial effects in various human diseases, particularly atherosclerosis and cancer (El-Seedi et al 2012;RazzaghiAsl et al 2013).…”

Section: Heterologous Overexpression and Catalytic Properties Of Cac4h2mentioning

confidence: 99%

“…Cinnamate 4-hydroxylase (C4H, EC 1.14.13.11), a typical P450 protein, catalyzes the regiospecific para-hydroxylation of trans-cinnamic acid to form p-coumaric acid (Schalk et al 1999;Ehlting et al 2006). The C4H-catalyzed oxidation reaction was reported to be the rate-limiting step in the phenylpropanoid pathway (Alber and Ehlting 2012). In 1960s, the C4Hs from the leaves of spinach and the apical buds of pea seedlings were biochemically characterized by two independent research groups (Nair and Vining 1965;Russell and Conn 1967).…”

Section: Introductionmentioning

confidence: 99%

“…S1, Supplementary Materials). 4-Hydroxycinnamic acid, i.e., p-coumaric acid, is the first oxygenation product involved in the biosynthesis of phenylpropanoids (Schalk et al 1999;Ehlting et al 2006;Vogt 2010;Alber and Ehlting 2012;Shuab et al 2016). Cinnamate 4-hydroxylase (C4H, EC 1.14.13.11), a typical P450 protein, catalyzes the regiospecific para-hydroxylation of trans-cinnamic acid to form p-coumaric acid (Schalk et al 1999;Ehlting et al 2006).…”

Section: Introductionmentioning

confidence: 99%

“…These biopolymers play an important role in the construction of plant structure, development, and defense for mechanical or environmental damage, like drought or wounding (Schalk et al 1999;Ehlting et al 2006;Vogt 2010;Alber and Ehlting 2012). The upstream part of the phenylpropanoid metabolism consists of three enzymatic steps leading to 4-coumaroyl CoA from L-phenylalanine (Fig.…”

Section: Introductionmentioning

confidence: 99%

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Molecular cloning and functional characterization of a cinnamate 4-hydroxylase-encoding gene from Camptotheca acuminata

Yang

Jiang

et al. 2016

Acta Physiol Plant

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Cinnamate 4-hydroxylase (C4H) catalyzes the regioselective para-hydroxylation of trans-cinnamic acid to form p-coumaric acid, the biosynthetic precursor of phenylpropanoid-based polymers. These biopolymers play an essential role in plant structure construction, development, and defense. Herein the open reading frame of CaC4H2 was cloned from Camptotheca acuminata, a deciduous camptothecin-producing tree native to China. CaC4H2 showed 94 % amino acid residues identity with those of reported CaC4H, which suggested that CaC4H2 is an isoform of C4Hs presented in C. acuminata. The intact CaC4H2 was overexpressed in Escherichia coli with its functional reaction partner cytochrome P450 reductase, CamCPR, which transfers electrons from NADPH to CaC4H2 to support the catalytic hydroxylation activity of CaC4H2. Upon incubating trans-cinnamic acid with the recombinant CaC4H2 and tCamCPR, the formation of pcoumaric acid was confirmed by the HPLC-DAD and UPLC-DAD-ESIMS analyses, which indicated the catalytic hydroxylation activity of CaC4H2. Quantitative realtime PCR analyses showed that CaC4H2 was expressed in all tissues of C. acuminata seedlings, which is consistent with the well-known conclusion that the C4H-catalyzed hydroxylation reaction is a key step within the biosynthetic pathway of phenylpropanoids. The functional characterization of CaC4H2 will be useful for molecular breeding and sustainable utilization and protection of the camptothecin-producing plant.

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