Ward, Lucy C.; McCue, Hannah V.; Rigden, Daniel J.; Kershaw, Neil M.; Ashbrook, Chloe; Hatton, Harry; Goulding, Ellie; Johnson, James R.; Carnell, Andrew J. published the artcile< Carboxyl Methyltransferase Catalysed Formation of Mono- and Dimethyl Esters under Aqueous Conditions: Application in Cascade Biocatalysis>, Product Details of C19H34O2, the main research area is Aspergillus carboxyl methyltransferase biocatalysis monomethyl dimethyl esters; Biocatalysis; Carboxylic Acids; Cascades; Enzymes; Methyltransferase.
Carboxyl methyltransferase (CMT) enzymes catalyze the biomethylation of carboxylic acids under aqueous conditions and have potential for use in synthetic enzyme cascades. Herein we report that the enzyme FtpM from Aspergillus fumigatus can methylate a broad range of aromatic mono- and dicarboxylic acids in good to excellent conversions. The enzyme shows high regioselectivity on its natural substrate fumaryl-L-tyrosine, trans, trans-muconic acid and a number of the dicarboxylic acids tested. Dicarboxylic acids are generally better substrates than monocarboxylic acids, although some substituents are able to compensate for the absence of a second acid group. For dicarboxylic acids, the second methylation shows strong pH dependency with an optimum at pH 5.5-6. Potential for application in industrial biotechnol. was demonstrated in a cascade for the production of a bioplastics precursor (FDME) from bioderived 5-hydroxymethylfurfural (HMF).
Angewandte Chemie, International Edition published new progress about Aspergillus fumigatus. 112-63-0 belongs to class esters-buliding-blocks, and the molecular formula is C19H34O2, Product Details of C19H34O2.
Referemce:
Ester – Wikipedia,
Ester – an overview | ScienceDirect Topics