Disease relevance of Coniferol

• The gene loci ehyA and ehyB, which are involved in the bioconversion of eugenol to coniferyl alcohol by Pseudomonas sp. strain HR199 (DSM 7063), were identified as the structural genes of a eugenol hydroxylase that represents an enzyme of the flavocytochrome c class [1].
• A bacterial isolate identified as Xanthomonas sp. proved to be ligninolytic due to its ability to degrade 14C-labeled dehydropolymers of coniferyl alcohol (DHP) and [14C]lignocellulose complexes from corn plants (Zea mays) [2].
• Several Nocardia and Pseudomonas spp., as well as some unidentified bacteria, isolated from lake water containing high loads of waste lignin, were tested for their capacity to release 14CO2 from specifically 14C-labelled dehydropolymer of coniferyl alcohol (DHP) or corn stalk lignins [3].
• Upon incubation of Rhizobium rhizogenes A4 with coniferyl alcohol, a lignin precursor, bacterial virulence on cotton cotyledon slices was stimulated [4].
• Coevolutionary toxicity as suggested by differential coniferyl alcohol inhibition of ceratocystis species growth [5].

Psychiatry related information on Coniferol

• Mn catalysts were found to oxidize coniferyl alcohol in a same reaction time as horseradish peroxidase (HRP) enzyme and Mn and Co catalysts showed different regioselectivity suggesting a different substrate to catalyst interaction in the oxidative coupling [6].

High impact information on Coniferol

• Provision of increasing levels of exogenously supplied Phe to saturating levels (40 mm) to the induction medium resulted in further up-regulation of their transcript levels in the P. taeda cell cultures; this in turn was accompanied by considerable increases in both p-coumaryl and coniferyl alcohol formation and excretion [7].
• Petunia flower petals emit large amounts of isoeugenol, which has been shown to be synthesized by isoeugenol synthase (PhIGS1) from an ester of coniferyl alcohol, hypothesized to be coniferyl acetate [8].
• UV-B exposure preferentially enhanced guaiacol-peroxidases, ascorbate peroxidase, and peroxidases specific to coniferyl alcohol and modified the substrate affinity of ascorbate peroxidase [9].
• A marked degree of physical interaction was detected between the enzymatic binding sites of the coniferyl alcohol substrate and the 2'-phosphate binding region, which are quite distant in the three-dimensional structure [10].
• Images generated using the 1,650 cm(-1) band showed that coniferaldehyde and coniferyl alcohol distribution followed that of lignin and no particular cell wall layer/region was therefore enriched in the ethylenic residue [11].

Chemical compound and disease context of Coniferol

• Among them, vanillic acid, vanillin and coniferyl alcohol showed significant inhibitory effects on bone resorption [12].

Biological context of Coniferol

• The enzyme shows a pronounced substrate specificity towards UDPglucose and coniferyl alcohol with Km values of respectively 220 microM and 250 microM [13].
• Crude cell wall preparations from Cicer arietinum L. cell suspension cultures show high activity for the hydrolysis of coniferyl alcohol beta-D-glucoside (coniferin) [14].
• Aggregation during coniferyl alcohol polymerization in pectin solution: a biomimetic approach of the first steps of lignification [15].
• However, the introduction of the fluorine atom at the terminal carbon atom of the double bond favors the ring hydroxylation over a side-chain metabolic oxidation pathway, by which coniferyl alcohol is produced [16].
• Resting cells of Amycolatopsis sp. HR167 (pRLE6SKvaom) produced coniferyl alcohol from eugenol with a maximum conversion rate of about 2.3 mmol/h/l of culture, and a maximum coniferyl alcohol concentration of 4.7 g/1 was obtained after 16 h biotransformation without further optimization [17].

Anatomical context of Coniferol

• A diffusion cell was used to allow the diffusion of both hydrogen peroxide and coniferyl alcohol into the peroxidase impregnated cellulose mats through dialysis membranes [18].

Associations of Coniferol with other chemical compounds

• On the other hand, CAD activity measured for coniferyl alcohol formation was transiently decreased but a substrate-specific activation of CAD activity was observed in F. oxysporum-treated cells when using sinapyl alcohol as substrate [19].
• In an in vitro enzyme assay, the developing mutant seeds showed a significant reduction in polymerization activity of coniferyl alcohol in the absence of H(2)O(2) [20].
• The oxidation of coniferyl alcohol (CA), a lignin precursor, by cell wall peroxidases may take place at the expense of indole-3-acetic acid (IAA) and O2, and in the absence of H2O2 [21].
• The cell wall localization of coniferin beta-glucosidase, the enzyme responsible for cleaving glucose from coniferin to generate free coniferyl alcohol, provides a mechanism to de-glucosylate monolignols in muro [22].
• Oxidation of coniferyl alcohol by cell wall peroxidases at the expense of indole-3-acetic acid and O2. A model for the lignification of plant cell walls in the absence of H2O2 [21].

Gene context of Coniferol

• Lignin peroxidase from a white-rot basidiomycete, Phanerochaete chrysosporium, catalyzed cleavages of the aromatic ring and the beta-O-4 bond of a synthetic lignin, a dehydrogenation copolymer (DHP) of coniferyl alcohol and a (beta-O-4)-(beta-beta) lignin substructure model trimer [23].
• Results also showed that the oxidase activity of this peroxidase is due to an evolutionarily gained optimal adaptation of the enzyme to the microM H(2)O(2) concentrations generated during the auto-oxidation of coniferyl alcohol, the stoichiometry of the chemical reaction (mol coniferyl alcohol auto-oxidized/mol H(2)O(2) formed) being 0.496 [24].
• We have characterized two H2O2-independent phenoloxidases with approximate molecular masses of 90 kDa and 110 kDa from cell walls of Populus euramericana xylem that are capable of oxidizing coniferyl alcohol [25].
• The ZPO-C:6xHis protein had a peroxidase activity preferring sinapyl alcohol as well as coniferyl alcohol as a substrate, with a narrow pH optimum around 5.25 [26].
• When coniferyl alcohol was the unique HRP substrate, three major dimers were observed (beta-5, beta-beta, and beta-O-4 interunit linkages) and their initial formation velocity as well as their relative abundance varied with pH [27].

Analytical, diagnostic and therapeutic context of Coniferol

• Analysis of the culture medium by HPLC and GC-MS showed that coniferyl alcohol, coniferaldehyde, and sinapyl alcohol accumulated in TE inductive culture [28].
• The dehydrogenative polymerization of coniferyl alcohol by horseradish peroxidase was performed in 0.10 M phosphate buffer at 27 degrees C. Dehydrogenative polymer (DHP) from coniferyl alcohol was characterized by size exclusion chromatography (SEC) and nuclear magnetic resonance (NMR) spectroscopy [29].

References