Disease relevance of Styrylcarbinol

• Transgenic poplars (Populus tremula x Populus alba) were obtained by introduction of a sense homologous transgene encoding caffeic acid O-methyltransferase (COMT) under the control either of the cauliflower mosaic virus double 35S promoter or of the eucalyptus cinnamyl alcohol dehydrogenase promoter [1].
• Characterization of cinnamyl alcohol dehydrogenase of Helicobacter pylori. An aldehyde dismutating enzyme [2].
• The gene for cinnamyl alcohol dehydrogenase from Helicobacter pylori (HpCAD) was cloned in Escherichia coli and the recombinant enzyme characterized for substrate specificity [2].

High impact information on Styrylcarbinol

• Wild-type Arabidopsis has a guaiacyl-rich, syringyl-guaiacyl lignin typical of other dicots, with prominent beta-aryl ether (beta-O-4), phenylcoumaran (beta-5), resinol (beta-beta), biphenyl/dibenzodioxocin (5-5), and cinnamyl alcohol end-group structures [3].
• Inheritance, gene expression, and lignin characterization in a mutant pine deficient in cinnamyl alcohol dehydrogenase [4].
• The coordinated up-regulation of phenylalanine ammonia lyase, 4-coumarate:CoA ligase, caffeoyl-CoA O-methyltransferase, cinnamoyl-CoA reductase and cinnamyl alcohol dehydrogenase in the presence of increasing concentrations of Phe also indicates that these steps are not truly rate-limiting, because they are modulated according to metabolic demand [5].
• These polymers arise from the oxidative coupling of three cinnamyl alcohols in a nonrandom reaction, in which cell wall polysaccharides appear to influence the freedom of cinnamyl alcohol radicals, giving rise to a highly orchestrated process [6].
• One of the genes, CAD, common to both systems and encoding the lignin-related protein cinnamyl alcohol dehydrogenase, was immunolocalized to immature xylem cells of the vascular bundles in the strawberry receptacle [7].

Biological context of Styrylcarbinol

• Nucleotide sequence of a cDNA encoding cinnamyl alcohol dehydrogenase from Eucalyptus [8].
• The work presented here suggests that there is a common hapten involved in cinnamaldehyde and cinnamic alcohol sensitization and that metabolic activation (to cinnamaldehyde) is involved in the latter [9].
• The overexpression of cad in the transgenic lines resulted in a down-regulation of cinnamyl alcohol dehydrogenase (EC 1.1.1.195) expression [10].
• A new enantioselective acylation catalyst (Cl-PIQ), designed to provide enhanced pi-stacking with benzylic and cinnamyl alcohol substrates, was found to give considerably increased reaction rates and selectivities compared with the first-generation catalyst CF(3)-PIP [11].
• The mRNA levels of a diverse array of gene products increases during leaf senescence, including a protease, a ribosomal protein, two cinnamyl alcohol dehydrogenases, a nitrilase and glyoxalase II [12].

Anatomical context of Styrylcarbinol

• The spectra of the ST activities for these odorants were similar in mouse nasal and liver cytosols, however, nasal cytosols showed much higher ST activity toward cinnamyl alcohol than liver cytosols [13].
• RESULTS: Differential metabolism of cinnamic alcohol and cinnamaldehyde was observed in various subcellular fractions: skin cytosol was seen to be the major site of cinnamic compound metabolism [14].

Associations of Styrylcarbinol with other chemical compounds

• Pathways for hydroxycinnamyl aldehyde incorporation into lignins are revealed by examining transgenic plants deficient in cinnamyl alcohol dehydrogenase, the enzyme that converts hydroxycinnamyl aldehydes to the hydroxycinnamyl alcohol lignin monomers [15].
• Cinnamoyl-CoA reductase and cinnamyl alcohol dehydrogenase were purified to apparent homogeneity from poplar stems (Populus euramericana) and their main properties were studied [16].
• Analysis of a crystal structure of alcohol dehydrogenase (Adh) from horse liver suggests that Trp54 in the homologous yeast alcohol dehydrogenase prevents the yeast enzyme from efficiently catalysing the oxidation of long-chain primary alcohols with branching at the 4 position (e.g. 4-methyl-1-pentanol, cinnamyl alcohol) [17].
• Cross-sensitization patterns in guinea pigs between cinnamaldehyde, cinnamyl alcohol and cinnamic acid [18].
• As the consumption rate of cinnamyl alcohol was much higher than production of rosin, the aqueous methanol extracts of compact callus aggregates were studied by liquid chromatography-mass spectrometric methods and four new unexpected biotransformation products of cinnamyl alcohol were identified [19].

Gene context of Styrylcarbinol

• Characterization of a Saccharomyces cerevisiae NADP(H)-dependent alcohol dehydrogenase (ADHVII), a member of the cinnamyl alcohol dehydrogenase family [20].
• It has been hypothesized that cinnamic alcohol is a "prohapten" that requires metabolic activation, presumably by oxidoreductase enzymes such as alcohol dehydrogenase (ADH) or cytochrome P450 2E1 (CYP2E1), to the protein-reactive cinnamaldehyde (a hapten) [21].
• Crystal structures and catalytic mechanism of the Arabidopsis cinnamyl alcohol dehydrogenases AtCAD5 and AtCAD4 [22].
• Identification and characterisation of cDNA clones encoding cinnamyl alcohol dehydrogenase from tobacco [23].
• The region on LG7 was associated with variation for all traits except CP, and is located in the vicinity of the lignin biosynthesis gene loci xlpomt1 (caffeic acid-O-methyltransferase), xlpccr1 (cinnamoyl CoA-reductase) and xlpssrcad 2.1 (cinnamyl alcohol dehydrogenase) [24].

Analytical, diagnostic and therapeutic context of Styrylcarbinol

• Chiral capillary electrophoresis applied to the determination of phenylglycidol enantiomers obtained from cinnamyl alcohol by asymmetric epoxidation using new titanium(IV) alkoxide compounds as catalysts [25].
• Molecular cloning and expression of a Eucalyptus gunnii cDNA clone encoding cinnamyl alcohol dehydrogenase [26].
• Molecular cloning, sequence analysis and elicitor-/ozone-induced accumulation of cinnamyl alcohol dehydrogenase from Norway spruce (Picea abies L.) [27].
• Simultaneous determination of phenylglycidol enantiomers and cinnamyl alcohol in asymmetric epoxidation processes by chiral liquid chromatography [28].
• A biolistic transformation procedure was used to transform embryogenic Pinus radiata tissue with constructs containing the Zea mays UBI1 (ubiquitin)-promoter followed by the P. radiata CAD (cinnamyl alcohol dehydrogenase) cDNA in sense or anti-sense orientation or in the form of an inverted-repeat [29].

References