Changes in Cell Wall Polymers and Degradability in Maize Mutants Lacking 3'- and 5'-O-Methyltransferases Involved in Lignin Biosynthesis.

doi:10.1093/pcp/pcw198

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Back to search

Article

Changes in Cell Wall Polymers and Degradability in Maize Mutants Lacking 3'- and 5'-O-Methyltransferases Involved in Lignin Biosynthesis.

Plant & cell physiology - 1 Feb 2017

Fornalé Silvia, Rencoret Jorge, García-Calvo Laura, Encina Antonio, Rigau Joan, Gutiérrez Ana, Del Río José Carlos, Caparros-Ruiz David

Abstract excerpt

Caffeoyl coenzyme A 3-O-methyltransferase (CCoAOMT) and caffeic acid-O-methyltransferase (COMT) are key enzymes in the biosynthesis of coniferyl and sinapyl alcohols, the precursors of guaiacyl (G) and syringyl (S) lignin subunits. The function of these enzymes was characterized in single and double mutant maize plants. In this work, we determined that the comt (brown-midrib 3) mutant plants display a reduction...

Topics

Cell Wall
Flavonoids
Methyltransferases
Mutation
Plant Proteins
Polymers
Polysaccharides
Zea mays

Source

Open in PubMed

Identifiers

PMID: 28013276
DOI: 10.1093/pcp/pcw198

Genes

COMT

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026.

Community interpretation

Discuss the evidence

Ask a question, add context or challenge an interpretation. Community activity is separate from scientific evidence strength.

discussions

replies

Citations encouraged

Claims remain attributable.

No discussion yet

Be the first to add a careful, cited interpretation.

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics