4-Coumarate 3-hydroxylase in the lignin biosynthesis pathway is a cytosolic ascorbate peroxidase
4-Coumarate 3-hydroxylase in the lignin biosynthesis pathway is a cytosolic ascorbate peroxidase
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Author / Creator
Barros, Jaime , Escamilla-Trevino, Luis , Song, Luhua , Rao, Xiaolan , Serrani-Yarce, Juan Carlos , Palacios, Maite Docampo , Engle, Nancy , Choudhury, Feroza K. , Tschaplinski, Timothy J. , Venables, Barney J. , Mittler, Ron , Dixon, Richard A. and Oak Ridge National Laboratory (ORNL), Oak Ridge, TN (United States)
Publisher
London: Nature Publishing Group UK
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English
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London: Nature Publishing Group UK
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Contents
Lignin biosynthesis is evolutionarily conserved among higher plants and features a critical 3-hydroxylation reaction involving phenolic esters. However, increasing evidence questions the involvement of a single pathway to lignin formation in vascular plants. Here we describe an enzyme catalyzing the direct 3-hydroxylation of 4-coumarate to caffeate...
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Full title
4-Coumarate 3-hydroxylase in the lignin biosynthesis pathway is a cytosolic ascorbate peroxidase
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TN_cdi_doaj_primary_oai_doaj_org_article_1eadfa8fa292476095ef6d6f823b767e
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https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_doaj_primary_oai_doaj_org_article_1eadfa8fa292476095ef6d6f823b767e
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ISSN
2041-1723
E-ISSN
2041-1723
DOI
10.1038/s41467-019-10082-7
