COA of Formula: C9H8O4On October 2, 2020 ,《An Enzyme Model Which Mimics Chymotrypsin and N-Terminal Hydrolases》 was published in ACS Catalysis. The article was written by Garrido-Gonzalez, Jose J.; Iglesias Aparicio, Ma Mercedes; Garcia, Miguel Martinez; Simon, Luis; Sanz, Francisca; Moran, Joaquin R.; Fuentes de Arriba, Angel L.. The article contains the following contents:
Enzymes are the most efficient and specific catalysts to date. Although they have been thoroughly studied for years, building a true enzyme mimic remains a challenging and necessary task. Here, we show how a three-dimensional geometry anal. of the key catalytic residues in natural hydrolases has been exploited to design and synthesize small-mol. artificial enzymes which mimic the active centers of chymotrypsin and N-terminal hydrolases. The optimized prototype catalyzes the methanolysis of the acyl enzyme mimic with a half-life of only 3.7 min at 20 °C, and it is also able to perform the transesterification of vinyl acetate at room temperature DFT studies and X-ray diffraction anal. of the catalyst bound to a transition state analog proves the similarity with the geometry of natural hydrolases. The experimental part of the paper was very detailed, including the reaction process of 3-(Methoxycarbonyl)benzoic acid(cas: 1877-71-0COA of Formula: C9H8O4)
3-(Methoxycarbonyl)benzoic acid(cas: 1877-71-0) belongs to esters. Esters are more polar than ethers but less polar than alcohols. COA of Formula: C9H8O4 They participate in hydrogen bonds as hydrogen-bond acceptors, but cannot act as hydrogen-bond donors, unlike their parent alcohols.
Referemce:
Ester – Wikipedia,
Ester – an overview | ScienceDirect Topics