Gall, Daniel L’s team published research in Environmental Science & Technology in 2014-10-21 | 112-63-0

Environmental Science & Technology published new progress about Hydrolysis, stereoselective. 112-63-0 belongs to class esters-buliding-blocks, and the molecular formula is C19H34O2, Product Details of C19H34O2.

Gall, Daniel L.; Ralph, John; Donohue, Timothy J.; Noguera, Daniel R. published the artcile< A Group of Sequence-Related Sphingomonad Enzymes Catalyzes Cleavage of β-Aryl Ether Linkages in Lignin β-Guaiacyl and β-Syringyl Ether Dimers>, Product Details of C19H34O2, the main research area is sphingomonad glutathione transferase aryl ether linkage lignin guaiacyl syringyl.

Lignin biosynthesis occurs via radical coupling of guaiacyl and syringyl hydroxycinnamyl alc. monomers (i.e., “”monolignols””) through chem. condensation with the growing lignin polymer. With each chain-extension step, monolignols invariably couple at their β-positions, generating chiral centers. Here, we report on activities of bacterial glutathione-S-transferase (GST) enzymes that cleave β-aryl ether bonds in lignin dimers that are composed of different monomeric units. Our data reveal that these sequence-related enzymes from Novosphingobium sp. strain PP1Y, Novosphingobium aromaticivorans strain DSM12444, and Sphingobium sp. strain SYK-6 have conserved functions as β-etherases, catalyzing cleavage of each of the four dimeric α-keto-β-aryl ether-linked substrates (i.e., guaiacyl-β-guaiacyl, guaiacyl-β-syringyl, syringyl-β-guaiacyl, and syringyl-β-syringyl). Although each β-etherase cleaves β-guaiacyl and β-syringyl substrates, we have found that each is stereospecific for a given β-enantiomer in a racemic substrate; LigE and LigP β-etherase homologs exhibited stereospecificity toward β(R)-enantiomers whereas LigF and its homologs exhibited β(S)-stereospecificity. Given the diversity of lignin’s monomeric units and the racemic nature of lignin polymers, we propose that bacterial catabolic pathways have overcome the existence of diverse lignin-derived substrates in nature by evolving multiple enzymes with broad substrate specificities. Thus, each bacterial β-etherase is able to cleave β-guaiacyl and β-syringyl ether-linked compounds while retaining either β(R)- or β(S)-stereospecificity.

Environmental Science & Technology published new progress about Hydrolysis, stereoselective. 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