Recent Advances in Lignan OMT Studies

Umezawa, Toshiaki; Yamamura, Masaomi; Ono, Eiichiro; Shiraishi, Akira; Ragamustari, Safendrri Komara

doi:10.2488/jwrs.65.1

Cited by 5 publications

(1 citation statement)

References 72 publications

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“…While the group Pl-OMT I (Joshi and Chiang 1998; also named Type 2 OMT by Noel et al 2003 andLineage A by Lam et al 2007) includes CCoAOMT and carboxyl OMTs, the group Pl-OMT II (Joshi and Chiang 1998; also named Type 1 OMT by Noel et al 2003 andLineage B by Lam et al 2007) contains Arabidopsis coniferaldehyde OMT 1 (CAldOMT1) (Nakatsubo et al 2008) and is more diverse. Previously identified lignan OMTs are all classified as Pl-OMT I (Lau and Sattely 2015;Ragamustari et al 2013Ragamustari et al , 2014Umezawa et al 2013Umezawa et al , 2019. We checked which previously identified lignan OMTs shared the highest E-value with T. dolabrata var.…”

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De novo transcriptome analysis of needles of Thujopsis dolabrata var. hondae

Suzuki

Tanaka

et al. 2019

Plant Biotechnology

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Podophyllotoxin is a starting material of the semisynthetic anticancer medicines etoposide, teniposide, and etopophos. The major plant source of podophyllotoxin is rhizomes of Podophyllum hexandrum, which is a Himalayan endangered species; therefore, alternative sources of podophyllotoxin or bioproduction systems have been pursued to avoid exploiting this limited natural resource. In this paper, we report de novo transcriptome analysis of Thujopsis dolablata var. hondae, which accumulates the podophyllotoxin derivatives (deoxypodophyllotoxin and β-peltatin A methyl ether) in its needles. We analyzed transcriptomes of the T. dolablata var. hondae young needles to obtain the sequences that putatively encode O-methyltransferases, cytochrome P450s, and a 2-oxoglutarate dependent dioxygenase because these protein families are responsible for podophyllotoxin-related compound formation in P. hexandrum. The resulting transcriptomes contained considerable numbers of coding sequences classified into the three protein families. Our results are a genetic basis for identifying genes involved in the biosynthesis of podophyllotoxin and related compounds and also for future metabolic engineering of podophyllotoxin in heterologous hosts.

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confidence: 99%

De novo transcriptome analysis of needles of Thujopsis dolabrata var. hondae

Suzuki

Tanaka

et al. 2019

Plant Biotechnology

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Chemistry of plant extracts

Rashmi

Negi

2022

Plant Extracts: Applications in the Food Industry

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Multifunctional 5-hydroxyconiferaldehydeO-methyltransferases (CAldOMTs) in plant metabolism

Lam,

Lui,

Bartley

et al. 2024

Journal of Experimental Botany

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Lignin, flavonoids, melatonin, and stilbenes are plant specialized metabolites with diverse physiological and biological functions, supporting plant growth and conferring stress resistance. Their biosynthesis requires O-methylations catalyzed by 5-hydroxyconiferaldehyde O-methyltransferase (CAldOMT; also called caffeic acid O-methyltransferase, COMT). CAldOMT was first known for its roles in syringyl (S) lignin biosynthesis in angiosperm cell walls and later found to be multifunctional. This enzyme also catalyzes O-methylations in flavonoid, melatonin, and stilbene biosynthetic pathways. Phylogenetic analysis indicated the convergent evolution of enzymes with OMT activities towards the monolignol biosynthetic pathway intermediates in some gymnosperm species that lack S-lignin and Selaginella moellendorffii, a lycophyte which produces S-lignin. Furthermore, neofunctionalization of CAldOMTs occurred repeatedly during evolution, generating unique O-methyltransferases (OMTs) with novel catalytic activities and/or accepting novel substrates, including lignans, 1,2,3-trihydroxybenzene, and phenylpropenes. This review summarizes multiple aspects of CAldOMTs and their related proteins in plant metabolism and discusses their evolution, molecular mechanism, and roles in biorefineries, agriculture, and synthetic biology.

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Recent Advances in Lignan OMT Studies

Cited by 5 publications

References 72 publications

<i>De novo</i> transcriptome analysis of needles of <i>Thujopsis dolabrata</i> var. <i>hondae</i>

<i>De novo</i> transcriptome analysis of needles of <i>Thujopsis dolabrata</i> var. <i>hondae</i>

Chemistry of plant extracts

Multifunctional 5-hydroxyconiferaldehydeO-methyltransferases (CAldOMTs) in plant metabolism

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