Lanostenyl benzoate

Paraoxonase 1 (PON1) can metabolize some compounds such as aromatic carboxylic acid and unsaturated aliphatic esters, arylesters, cyclic carbonate, plucuronide drugs, some carbamate insecticide classes, nerve gases, and lactone compounds. Methyl benzoate has recently been shown to display potent toxicity against several insect species. In the current study, we aimed to investigate the effect of the methyl benzoate compounds (1-17) on PON1 activity. Methyl benzoate compounds inhibited PON1 with KI values ranging from 25.10 ± 4.73 to 502.10 ± 64.72 μM. Compound 10 (methyl 4-amino-2-bromo benzoate) showed the best inhibition (KI = 25.10 ± 4.73 μM). Furthermore, using the ADME-Tox, Glide XP, and MM-GBSA tools of the Schrödinger Suite 2021-4, a complete ligand-receptor interaction prediction was performed to characterize the methyl benzoates (1-17), probable binding modalities versus the PON1.

Background: Halogenated aromatic compounds are more resistant to microbial degradation than non-halogenated aromatic compounds. Microbial degradation of sodium benzoate in the presence of sodium 3-chlorobenzoate is of interest. The ability to degrade aromatic compounds is largely determined by the substrate specificity of the first enzyme that initiates degradation, namely, benzoate 1,2-dioxygenase for benzoate degradation, and 3-chlorobenzoate 1,2-dioxygenase for 3-chlorobenzoate degradation. In this study, the perspective of immobilized cells of Rhodococcus opacus 1CP actinobacterium for degradation of benzoate and 3-chlorobenzoate was explored. Methods: The biosensor approach (a membrane microbial sensor based on immobilized cells of Rhodococcus opacus 1CP and the Clark-type oxygen electrode as a transducer) was applied to evaluate the actinobacterial cells' responses to benzoate and 3-chlorobenzoate in the absence of both enzymes, benzoate 1,2-dioxygenase and 3-chlorobenzoate 1,2-dioxygenase, or in the presence of one of the said enzymes. Results: Data obtained show that 1CP actinobacterium possessed a constitutive system for the transport of benzoate and 3-chlorobenzoate into culture cells. The affinity of the transport system for benzoate was higher than that for 3-chlorobenzoate. Moreover, adaptation to one substrate did not preclude the use of the second substrate. Probably, porins facilitated the penetration of benzoate and 3-chlorobenzoate into 1CP cells. Analyzing V vs. S dependencies, negative cooperativity was found, when benzoate 1,2-dioxygenase bound substrate (3-chlorobenzoate), while positive cooperativity was determined at benzoate binding. The observed difference could be associated with the presence of at least two systems of 3-chlorobenzoate transport into actinobacterial cells and allosteric interaction of active sites of benzoate 1,2-dioxygenase in the presence of 3-chlorobenzoate. Conclusions: The membrane microbial sensor based on immobilized Rhodococcus opacus 1CP cells could be useful as a perspective tool for comparative evaluation of enzymes of complex structure such as benzoate- and 3-chlorobenzoate 1,2-dioxygenase.

A norbisabolane and an arabitol benzoate, Talaromarnine A (1), Talaromarnine B (2), together with eight known compounds were obtained from cultures of Talaromyces marneffei, an endophytic fungus of Epilobium angustifolium. Their structures were elucidated by IR, MS, 1D and 2D NMR spectra, and their absolute configuration was determined by single-crystal X-ray diffraction and molecular computation. These compounds were tested for monoamine oxidase, acetylcholinesterase and PI3K inhibitory activity, but no compounds exhibited significant activities.