488-20-0

Basic information

• Product Name: dimethylidenebutanedioic acid
• CAS NO: 488-20-0
• Molecular Formula: C₆H₆O₄
• Molecular Weight: 142.1094
• Mol File: 488-20-0.mol
• Article Data: 4

Chemical Properties

• Boiling Point: 361.2°C at 760 mmHg
• Flash Point: 186.4°C
• Density: 1.332g/cm³
• Vapor Pressure: 3.37E-06mmHg at 25°C
• Refractive Index: 1.514
• CAS DataBase Reference: dimethylidenebutanedioic acid(CAS DataBase Reference)
• NIST Chemistry Reference: dimethylidenebutanedioic acid(488-20-0)
• EPA Substance Registry System: dimethylidenebutanedioic acid(488-20-0)

Safety Data

• Hazardous Substances Data: 488-20-0(Hazardous Substances Data)

Upstream product

• 92960-19-5 Diacetyl-2,3-dimethyl-weinsaeure-dimethylester 
• 51865-23-7 2,3-Bis-piperidin-1-ylmethyl-succinic acid diethyl ester; hydrochloride 
• 74956-34-6 meso-2,3-Dimethyl-weinsaeure-dimethylester 
• 18216-47-2 2,3-dicyano-2,3-butanediol 
• 56575-56-5 4-bromo-but-1-ene-2,3-dicarboxylic acid 
• 934167-64-3 di-tert-butyl buta-1,3-diene-2,3-dicarboxylate 
• 245124-18-9 3-Hydroxymethyl-4-methylfuran-2,5-dione 
• 98453-81-7 2-(bromomethyl)-3-methyl maleic anhydrate 
• 41793-20-8 diethyl bis(methylene)butanedioate 
• 38818-30-3 dimethyl 1,3-butadiene-2,3-dicarboxylate 

Relevant articles and documents

Mechanism-based inactivation of coenzyme B12-dependent 2-methyleneglutarate mutase by (Z)-glutaconate and buta-1,3-diene-2,3- dicarboxylate

In the presence of holo 2-methyleneglutarate mutase, buta-1,3-diene-2,3- dicarboxylate and (Z)-glutaconate [(Z)-pent-2-ene-1,5-dicarboxylate], but not (E)-glutaconate, each induced homolysis of the Co-C bond of coenzyme B 12 to afford cob(II)alamin and the 5′-deoxyadenosyl radical. The latter probably added to the double bond in (Z)-glutaconate and one of the double bonds in buta-1,3-diene-2,3-dicarboxylate to afford a corresponding "radical adduct". The formation of new radicals and cob(II)alamin was diagnosed by UV/Visible and EPR spectroscopy. (Z)-Glutaconate rapidly inactivated the mutase with formation of aquocobalamin, which was possibly derived by electron transfer from cob(II)alamin to the radical adduct. In contrast, buta-1,3-diene-2,3-dicarboxylate was a much slower inactivator. In this case, the spectroscopic data revealed a relatively stable complex of the radical adduct with cob(II)alamin in the active site of the enzyme. Wiley-VCH Verlag GmbH & Co. KGaA, 2006.

The mechanism of action of vitamin B12

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