4219-47-0Relevant articles and documents
COMPOSITIONS COMPRISING ENZYME CLEAVABLE LINKER PLATFORMS AND CONJUGATES THEREOF
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Page/Page column 49; 50, (2021/01/23)
The present invention relates to a cleavable linker platform. In particular, the invention relates to construction of an enzyme cleavable linker platform conjugated to a drug or a diagnostically relevant compound, a biomolecule, and an enzyme cleavable group, for which cleavage of the enzyme cleavable group leads to release of the drug or diagnostically relevant compound.
Kinetics and quantitative structure-activity relationships for pseudomonas sp. Lipase-catalyzed hydrolysis of both monoesters and diesters of ethylene glycol
Chiou, Shyh-Ying,Cheng, Yu-Ru,Lu, Chun-Ping,Lin, Yan-Fu,Lin, Long-Yau,Lin, Gialih
, p. 201 - 207 (2007/10/03)
The goal of this work is to study kinetics and quantitative structure-activity relationships for steady states of Pseudomonas sp. lipase-catalyzed hydrolysis of both diesters and monoesters of ethylene glycol. Based on the steady-state kinetics of the enzyme-catalyzed hydrolysis of the diesters of ethylene glycol, the diesters and the monoesters react simultaneously as soon as monoester has started to build up in the reaction medium. In other words, the apparent Km values of the diesters are the Km values of the diesters (KmA) plus the Km values of the monoesters (KmB), and all Vmax values are about the same. Moreover, the pH-stat titration curve of the enzyme-catalyzed hydrolysis of the diesters of ethylene glycol is initially hyperbolic, then there is a sharp falloff in the hydrolysis rate. The abrupt stoppage of the reaction (relaxation stage) may be due to the existence of two phases in the reaction medium, that is, the product (ethylene glycol) and the substrates (the diesters of ethylene glycol) are not miscible. Furthermore, quantitative structure-activity relationships for varied acyl groups of mono- and diesters of ethylene glycol are studied. The fact that both pKmA and pK mB values are linearly correlated with the hydrophobicity constant (π) but not with the electronic substituent constants (σ*) indicates that the affinity of these substrates for the enzyme depends only on the hydrophobicitv of substrates. Copyright
Cobalt(II) catalyzed oxidation of 2-substituted 1,3-dioxolanes with molecular oxygen
Li, Pei,Alper, Howard
, p. 84 - 89 (2007/10/02)
Cobalt(II) chloride catalyzed oxidation of 2-substituted 1,3-dioxolanes in 1,2-dimethoxyethane afforded formate esters and acids in high yields.Is was found that the presence of catalytic amounts of ZnCl2 increased the rate of oxidation.A free-radical mechanism is proposed, involving participation of superoxocobalt, and the esterification of the alcohol and acid.