Regulatory role of cinnamyl alcohol dehydrogenase in the formation of guaiacyl and syringyl lignins

1982 ◽  
Vol 21 (1) ◽  
pp. 19-23 ◽  
Author(s):  
Hidetoshi Kutsuki ◽  
Mikio Shimada ◽  
Takayoshi Higuchi
Keyword(s):  
Alcohol Dehydrogenase ◽  
Cinnamyl Alcohol Dehydrogenase ◽  
Regulatory Role ◽  
Cinnamyl Alcohol

Comparative efficiency of different constructs for down regulation of tobacco cinnamyl alcohol dehydrogenase

1998 ◽  
Vol 49 (2) ◽  
pp. 295-306 ◽  
Author(s):  
Nabila Yahiaoui, Christiane Marque ◽  
Hélène Corbière ◽  
Alain Michel Boudet
Keyword(s):  
Alcohol Dehydrogenase ◽  
Cinnamyl Alcohol Dehydrogenase ◽  
Cinnamyl Alcohol ◽  
Down Regulation ◽  
Comparative Efficiency

Sequence analysis and functional characterization of the promoter of the Picea glauca Cinnamyl Alcohol Dehydrogenase gene in transgenic white spruce plants

2009 ◽  
Vol 28 (5) ◽  
pp. 787-800 ◽  
Author(s):  
Frank Bedon ◽  
Caroline Levasseur ◽  
Jacqueline Grima-Pettenati ◽  
Armand Séguin ◽  
John MacKay
Keyword(s):  
Sequence Analysis ◽  
Alcohol Dehydrogenase ◽  
Picea Glauca ◽  
Functional Characterization ◽  
Cinnamyl Alcohol Dehydrogenase ◽  
White Spruce ◽  
Cinnamyl Alcohol ◽  
Dehydrogenase Gene

Isolation and characterization of cDNA encoding cinnamyl alcohol dehydrogenase (CAD) in sorghum (Sorghum bicolor (L.) Moench)

2007 ◽  
Vol 53 (2) ◽  
pp. 103-109 ◽  
Author(s):  
Shin-ichi Tsuruta ◽  
Masumi Ebina ◽  
Hitoshi Nakagawa ◽  
Osamu Kawamura ◽  
Ryo Akashi
Keyword(s):  
Alcohol Dehydrogenase ◽  
Sorghum Bicolor ◽  
Cinnamyl Alcohol Dehydrogenase ◽  
Cinnamyl Alcohol ◽  
Isolation And Characterization ◽  
Sorghum Bicolor L

scholarly journals Structural Studies of Cinnamoyl-CoA Reductase and Cinnamyl-Alcohol Dehydrogenase, Key Enzymes of Monolignol Biosynthesis

2014 ◽  
Vol 26 (9) ◽  
pp. 3709-3727 ◽  
Author(s):  
H. Pan ◽  
R. Zhou ◽  
G. V. Louie ◽  
J. K. Muhlemann ◽  
E. K. Bomati ◽  
...  
Keyword(s):  
Alcohol Dehydrogenase ◽  
Cinnamyl Alcohol Dehydrogenase ◽  
Structural Studies ◽  
Cinnamyl Alcohol ◽  
Key Enzymes ◽  
Cinnamoyl Coa Reductase ◽  
Monolignol Biosynthesis ◽  
Coa Reductase

scholarly journals A Wheat Cinnamyl Alcohol Dehydrogenase TaCAD12 Contributes to Host Resistance to the Sharp Eyespot Disease

2016 ◽  
Vol 7 ◽  
Author(s):  
Wei Rong ◽  
Meiying Luo ◽  
Tianlei Shan ◽  
Xuening Wei ◽  
Lipu Du ◽  
...  
Keyword(s):  
Alcohol Dehydrogenase ◽  
Host Resistance ◽  
Cinnamyl Alcohol Dehydrogenase ◽  
Cinnamyl Alcohol ◽  
Eyespot Disease ◽  
Sharp Eyespot

Isolation and expression of a cinnamyl alcohol dehydrogenase cDNA from perennial ryegrass (Lolium perenne)

2001 ◽  
Vol 28 (11) ◽  
pp. 1085
Author(s):  
Fiona M. McAlister ◽  
Wendy R. Lewis-Henderson ◽  
Colin L. D. Jenkins ◽  
John M. Watson
Keyword(s):  
Alcohol Dehydrogenase ◽  
Lolium Perenne ◽  
Perennial Ryegrass ◽  
Blot Hybridization ◽  
Substrate Inhibition ◽  
Cinnamyl Alcohol Dehydrogenase ◽  
Southern Blot Hybridization ◽  
Leaf Sheath ◽  
Cinnamyl Alcohol ◽  
Degenerate Oligonucleotide

A perennial ryegrass (Lolium perenne L.) cDNA library was screened with a PCR-amplified cad DNA fragment generated from ryegrass cDNA template using degenerate oligonucleotide primers. A full-length cDNA (LpeCad1) was isolated and confirmed to encode a cinnamyl alcohol dehydrogenase (CAD) enzyme by expression of activity in Escherichia coli. The recombinant enzyme catalyses conversion of coniferaldehyde and sinapaldehyde with similar efficiency, and apparent K m values below 10 µM were determined for these substrates, whereas weak substrate inhibition occurs above this concentration. The predicted perennial ryegrass CAD was very similar (88–87percnt; amino acid sequence identity) to the only other monocotyledonous plant CAD sequences available, those of maize and sugarcane, respectively. Southern blot hybridization analysis indicated that there may be two or three cad genes, or alleles, in perennial ryegrass. The ryegrass LpeCad1 gene resembles the maize cadgene in showing strong expression in root and stem tissues, but is also expressed at lower levels in shoot, leaf sheath, leaf blade and floral tissues.

scholarly journals Isolation and Characterization of Full-Length Phenylalanine Ammonium Lyase and Cinnamyl Alcohol Dehydrogenase Genes Involved in Lignin Biosynthesis of Erianthus Arundinaceus

Proceedings ◽  
2020 ◽  
Vol 36 (1) ◽  
pp. 174
Author(s):  
Lakshmi Kasirajan ◽  
Prathima Perumal Thirugnanasambandam ◽  
Agnelo Furtado ◽  
Frikkie C. Botha ◽  
Robert J. Henry
Keyword(s):  
Alcohol Dehydrogenase ◽  
Untranslated Region ◽  
Plant Cell Wall ◽  
Lignin Content ◽  
Lignin Biosynthesis ◽  
Cinnamyl Alcohol Dehydrogenase ◽  
Raw Material ◽  
Sequence Information ◽  
Cinnamyl Alcohol ◽  
Isolation And Characterization

Lignocellulosic biomasses available in abundance is the most promising raw material for alternate energy production considering the issues of dwindling oil prices, and global warming. Recently, Erianthus arundinaceous has been identified as a potential target for second generation biofuel crop due to its high biomass production, and adaptability to extreme growth environments. Lignin is a major plant cell wall polymer indispensable for plant growth and development, however it hinders the saccharification of lignocellulosic biomass. Based on the previous transcriptome studies in a set of sugarcane genotypes differing for lignin content, genes encoding cinnamyl alcohol dehydrogenase (CAD), and Phenylalanine ammonia lyase (PAL) genes playing major roles in genetic regulation of lignin production have been cloned and characterized from an Erianthus clone IK 76-81. The genomic region of EriCAD was 3524 bp sequence containing four exons and three introns, among which the exon 1&2 of 88 and 80 bp were conserved with sorghum and Miscanthus CADs. The coding region of CAD was identified with 1086 bp open reading frame (ORF), a 68 bp 5′ untranslated region (UTR), and a 86 bp 3′ untranslated region (UTR). In the PROSITE analysis, a zinc-containing alcohol dehydrogenase signature (GHEVVGEVVEVGPEV) and an NADP-binding domain motif (GLGGLG) was identified. Similarly sequence analysis of PAL showed an ORF of 2106 bp encoding for 702 amino acid residues. It was flanked by 172 bp of 5′ UTR and 121 bp of 3′ UTR. This sequence information on PAL and CAD from Erianthus might be useful for subsequent research on lignin modification for improved biomass conversion.

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