ArticlePlant molecular biology2007
Catalytic activity, duplication and evolution of the CYP98 cytochrome P450 family in wheat.
Article in Plant molecular biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 52 citations in OpenAlex.
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- CYP98A monooxygenases: a key enzyme family in plant phenolic compound biosynthesis.Horticulture research · 2025Article
- Physiological mechanism of lodging resistance of oat stalk and analysis of transcriptome differences.Frontiers in plant science · 2025Article
- Cytochromes P450 evolution in the plant terrestrialization context.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2024Review
- Promiscuity, a Driver of Plant Cytochrome P450 Evolution?Biomolecules · 2023Review
- Spatial Genomic Resource Reveals Molecular Insights into Key Bioactive-Metabolite Biosynthesis in EndangeredInternational journal of molecular sciences · 2022Article
- Knockdown ofInternational journal of molecular sciences · 2022Article
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- Fluorescence from abnormally sterile pollen of the Japanese apricot.Plant biotechnology (Tokyo, Japan) · 2021Article
- Transcriptome Analysis Reveals genes involved in flavonoid biosynthesis and accumulation in Dendrobium catenatum From Different Locations.Scientific reports · 2018Article
- Differentially expressed genes in heads and tails of Angelica sinensis diels: Focusing on ferulic acid metabolism.Chinese journal of integrative medicine · 2017Article
- Early lignin pathway enzymes and routes to chlorogenic acid in switchgrass (Panicum virgatum L.).Plant molecular biology · 2014Article
- Plant P450s as versatile drivers for evolution of species-specific chemical diversity.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2013Review
- CYP98A22, a phenolic ester 3'-hydroxylase specialized in the synthesis of chlorogenic acid, as a new tool for enhancing the furanocoumarin concentration in Ruta graveolens.BMC plant biology · 2012Article
- Article
- A novel red clover hydroxycinnamoyl transferase has enzymatic activities consistent with a role in phaselic acid biosynthesis.Plant physiology · 2009Article
- Isolation and mapping of a C3'H gene (CYP98A49) from globe artichoke, and its expression upon UV-C stress.Plant cell reports · 2009Article
- cDNA cloning and functional characterisation of CYP98A14 and NADPH:cytochrome P450 reductase from Coleus blumei involved in rosmarinic acid biosynthesis.Plant molecular biology · 2009Article
- High-yield expression and purification of isotopically labeled cytochrome P450 monooxygenases for solid-state NMR spectroscopy.Biochimica et biophysica acta · 2007Article
- Functional characterization of two p-coumaroyl ester 3'-hydroxylase genes from coffee tree: evidence of a candidate for chlorogenic acid biosynthesis.Plant molecular biology · 2007Article
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Authors and funding
9 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A burst of evolutionary duplication upon land colonization seems to have led to the large superfamily of cytochromes P450 in higher plants. Within this superfamily some clans and families are heavily duplicated. Others, such as genes involved in the phenylpropanoid pathway have led to fewer duplication events. Eight coding sequences belonging to the CYP98 family reported to catalyze the 3-hydroxylation step in this pathway were isolated from Triticum aestivum (wheat) and expressed in yeast. Comparison of the catalytic properties of the recombinant enzymes with those of CYP98s from other plant taxa was coupled to phylogenetic analyses. Our results indicate that the unusually high frequency of gene duplication in the wheat CYP98 family is a direct or indirect result from ploidization. While ancient duplication led to evolution of enzymes with different substrate preferences, most of recent duplicates underwent silencing via degenerative mutations. Three of the eight tested CYP98s from wheat have phenol meta-hydroxylase activity, with p-coumaroylshikimate being the primary substrate for all of these, as it is the case for CYP98s from sweet basil and Arabidopsis thaliana. However, CYP98s from divergent taxa have acquired different additional subsidiary activities. Some of them might be significant in the metabolism of various free or conjugated phenolics in different plant species. One of the most significant is meta-hydroxylation of p-coumaroyltyramine, predominantly by the wheat enzymes, for the synthesis of suberin phenolic monomers. Homology modeling, confirmed by directed mutagenesis, provides information on the protein regions and structural features important for some observed changes in substrate selectivity. They indicate that the metabolism of quinate ester and tyramine amide of p-coumaric acid rely on the same recognition site in the protein.
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