Disease relevance of Meliotine

• 3,4-Dihydrocoumarin hydrolase with haloperoxidase activity from Acinetobacter calcoaceticus F46 [1].
• Studies on the mechanism of coumarin-induced toxicity in rat hepatocytes: comparison with dihydrocoumarin and other coumarin metabolites [2].
• Natural dihydrocoumarin, which is of great interest in the flavor industry, was biotechnologically produced from pure coumarin or tonka bean meal with Pseudomonas orientalis, Bacillus cereus, and various Saccharomyces cerevisiae strains [3].

High impact information on Meliotine

• XenA catalyses the NADPH-dependent reduction of 8-hydroxycoumarin and coumarin to produce 8-hydroxy-3,4-dihydrocoumarin and 3,4-dihydrocoumarin, respectively [4].
• The kinetic parameters of Vmax and Km for dihydrocoumarin hydrolysis by rhPON3 were 698+/-248 U/mg and 0.84+/-0.24 mM (n=3) [5].
• Role of Acinetobacter calcoaceticus 3,4-dihydrocoumarin hydrolase in oxidative stress defence against peroxoacids [6].
• Biocatalytic production of dihydrocoumarin from coumarin by Saccharomyces cerevisiae [3].
• Here we show that dihydrocoumarin (DHC), a compound found in Melilotus officinalis (sweet clover) that is commonly added to food and cosmetics, disrupted heterochromatic silencing and inhibited yeast Sir2p as well as human SIRT1 deacetylase activity [7].

Chemical compound and disease context of Meliotine

• The Acinetobacter calcoaceticus enzyme catalyzing the specific hydrolysis of dihydrocoumarin belongs to serine-enzyme family, and is useful for enantioselective hydrolysis of methyl DL-beta-acetylthioisobutyrate and regioselective hydrolysis of methyl cetraxate [8].

Biological context of Meliotine

• It is note-worthy that dihydrocoumarin II which carried an extra-aromatic group fitted well within the active site of light and heavy urokinases, suggesting a nonpolar character for their primary binding site [9].

Associations of Meliotine with other chemical compounds

• Based on the results of GC-MS analysis, an HPLC procedure was developed for the determination of coumarin, dihydrocoumarin, melilotic acid (o-dihydrocoumaric acid), methyl melilotate, ethyl melilotate, 5-hydroxymethylfurfural and o-coumaric acid which are characteristic compounds of tonka beans [10].

Gene context of Meliotine

• The extent of fibrin clot lysis induced by urokinase and two-chain tissue plasminogen activator was considerably decreased after treatment of these enzymes with the dihydrocoumarin derivative (molar excess of inhibitor over enzyme ranging from 6 to 21 for urokinase and 50 to 1500 for tissue plasminogen activator) [11].

References