63807-85-2

Basic information

• Product Name: Erythrinin C
• Synonyms: 2-(1-Methyl-1-hydroxyethyl)-4-hydroxy-6-(4-hydroxyphenyl)-2,3-dihydro-5H-furo[3,2-g][1]benzopyran-5-one;2,3-Dihydro-2-(1-hydroxy-1-methylethyl)-4-hydroxy-6-(4-hydroxyphenyl)-5H-furo[3,2-g][1]benzopyran-5-one;Erythrinin C;2,3-Dihydro-4-hydroxy-2-(1-hydroxy-1-methylethyl)-6-(4-hydroxyphenyl)-5H-furo[3,2-g][1]benzopyran-5-one;5H-Furo[3,2-g][1]benzopyran-5-one,2,3- dihydro-4-hydroxy-2-(1-hydroxy-1-Methylethyl)- 6-(4-hydroxyphenyl)-
• CAS NO: 63807-85-2
• Molecular Formula: C₂₀H₁₈O₆
• Molecular Weight: 354.35332
• Mol File: 63807-85-2.mol
• Article Data: 1

Chemical Properties

• Appearance: /
• CAS DataBase Reference: Erythrinin C(CAS DataBase Reference)
• NIST Chemistry Reference: Erythrinin C(63807-85-2)
• EPA Substance Registry System: Erythrinin C(63807-85-2)

Safety Data

• Hazardous Substances Data: 63807-85-2(Hazardous Substances Data)

Usage

General Description

Erythrinin C is a chemical compound that primarily originates from Erythrina species, a type of leguminous plants. It's a group of Erythrinin alkaloids that show various biological activities like anti-inflammatory properties, and they may serve a vital role in treating diseases associated with inflammation. Furthermore, the potency and level of Erythrinin C activity may vary depending upon the plant source and its extraction process. These compounds are commonly used in traditional medicine and are the subject of ongoing research for potential therapeutic applications.

Upstream product

• 51225-30-0 erythrinin B 

Relevant articles and documents

Fad-dependent epoxidase as a key enzyme in fungal metabolism of prenylated flavonoids

Crude protein extracts from Botrytis cinerea preincubated with 6- prenylnaringenin (6-PN) for 20 hr catalysed the prenyl epoxidation of 7-O- methyl-luteone. The resulting epoxide was non-enzymatically and slowly converted into the corresponding dihydrofurano derivative in a buffer solution at pH 7.5. Preparation of cell-free extracts in the presence of 6- PN from the mycelia without preincubation with 6-PN hardly showed the epoxidizing activity. These facts revealed that the substrate analogue 6-PN has a role as an enzyme inducer rather than stabilizer. The enzyme reaction depends on molecular oxygen and NADPH. Low amounts of FAD were necessary for maximal enzyme activity. The enzymatic activity was not inhibited by various inhibitors of cytochrome P-450 tested, in addition to carbon monoxide and cytochrome c. The results indicated that this enzyme does not belong to the monooxygenases dependent on cytochrome P-450, but to those dependent on FAD. About half of the total enzyme activity was found in the 125 000 g supernatant, but the specific activity for the epoxidation reaction in the 125 000 g pellet was 3.7-fold higher than in the soluble fraction. The enzyme showed high specificity to monoprenyl isoflavones. Finally, a preliminary experiment using a cell-free system from white lupin hypocotyls resulted in formation of small amounts of an epoxide corresponding to 7-O-methyl-luteone used as the substrate.