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

Article

The Enzyme Activity and Substrate Specificity of Two Major Cinnamyl Alcohol Dehydrogenases in Sorghum (Sorghum bicolor), SbCAD2 and SbCAD4.

Plant physiology - 1 Aug 2017

Jun Se-Young, Walker Alexander M, Kim Hoon, Ralph John, Vermerris Wilfred, Sattler Scott E, Kang ChulHee

Abstract excerpt

Cinnamyl alcohol dehydrogenase (CAD) catalyzes the final step in monolignol biosynthesis, reducing sinapaldehyde, coniferaldehyde, and p-coumaraldehyde to their corresponding alcohols in an NADPH-dependent manner. Because of its terminal location in monolignol biosynthesis, the variation in substrate specificity and activity of CAD can result in significant changes in overall composition and amount of lignin. Our...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Alcohol Oxidoreductases
Share to Catalytic Domain

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Crystallography, X-Ray

Share to Plant Proteins

Share to Protein Structure, Secondary

Share to Sorghum

Share to Substrate Specificity

Source

Open in PubMed Open full text

Identifiers

PMID: 28606901
DOI: 10.1104/pp.17.00576
PMCID: PMC5543964

Genes

CAD

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The Enzyme Activity and Substrate Specificity of Two Major Cinnamyl Alcohol Dehydrogenases in Sorghum (Sorghum bicolor), SbCAD2 and SbCAD4.PMID 28606901Read ↗

A genomewide analysis of the cinnamyl alcohol dehydrogenase family in sorghum [Sorghum bicolor (L.) Moench] identifies SbCAD2 as the brown midrib6 gene.Semantic proximity Read ↗

Structural and Biochemical Characterization of Cinnamoyl-CoA Reductases.Semantic proximity Read ↗

A nonsense mutation in a cinnamyl alcohol dehydrogenase gene is responsible for the Sorghum brown midrib6 phenotype.Semantic proximity Read ↗

Characterization of novel Brown midrib 6 mutations affecting lignin biosynthesis in sorghum.Semantic proximity Read ↗

Elucidation of the structure and reaction mechanism of sorghum hydroxycinnamoyltransferase and its structural relationship to other coenzyme a-dependent transferases and synthases.Semantic proximity Read ↗

Brown midrib2 (Bmr2) encodes the major 4-coumarate:coenzyme A ligase involved in lignin biosynthesis in sorghum (Sorghum bicolor (L.) Moench).Semantic proximity Read ↗

Evaluation of Brown Midrib Sorghum Mutants as a Potential Biomass Feedstock for 2,3-Butanediol Biosynthesis.Semantic proximity Read ↗

Map-based cloning and expression analysis of BMR-6 in sorghum.Semantic proximity Read ↗

CINNAMYL ALCOHOL DEHYDROGENASE-C and -D are the primary genes involved in lignin biosynthesis in the floral stem of Arabidopsis.Semantic proximity Read ↗

A Genomic Resource for the Development, Improvement, and Exploitation of Sorghum for Bioenergy.Semantic proximity Read ↗

Functional characterization of cinnamyl alcohol dehydrogenase and caffeic acid O-methyltransferase in Brachypodium distachyon.Semantic proximity Read ↗

Genetic complexity of miscanthus cell wall composition and biomass quality for biofuels.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.