Ферментативные Реакции В Химикоэнзиматическом Синтезе Лекарственных Препаратов (Обзор)

Bezborodov, A.M.; Am, Bezborodov; Загустина, Н. А.

doi:10.7868/s055510991603003x

Cited by 2 publications

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“…ХО относится к классу оксидоредуктаз, имеет молекулярную массу 55 кДа и катализирует окислительно-восстановительные реакции, в частности, окисление гидроксильного радикала ХС в положении С3 с образованием кетона (холест-4-ен-3-он) и пероксида водорода. ХО применяют в лабораторной диагностике для определения в сыворотке крови уровня общего холестерина (ХС) и ХС-липопротеинов высокой плотности (ХС-ЛПВП) энзиматическим методом в наборах фирмы "Vital Diagnostics" (Россия) [3]. Современное биотехнологическое использование ХО, получаемой из различных источников, её новые физико-химические и физиологические свойства активно изучаются во многих зарубежных лабораториях [4,5].…”

Section: Introductionunclassified

Effect of lipid-lowering activity of the natural original enzyme preparation in the experiment

et al. 2019

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The experimental study in vivo was aimed at evaluation of hypolipidemic action of the original natural microbial enzyme preparation of cholesterol oxidase (CHO). In preliminary chronic experiments in rats, rabbits, dogs, low toxicity, good tolerability, and anti-atherosclerotic activity of the CHO preparation were established. To assess the effect of CHO under conditions of moderate, nutritional, atherogenic dyslipoproteinemia, experiments were carried out in rats, guinea pigs, and rabbits. It was shown that administration of CHO had the pronounced lipid-lowering effect in models of atherogenic dyslipoproteinemia induced in these animals.

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Section: Introductionunclassified

Effect of lipid-lowering activity of the natural original enzyme preparation in the experiment

et al. 2019

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Promiscuous Catalytic Activity of a BinuclearMetallohydrolase: Peptide and Phosphoester Hydrolyses

Serafim

Jayasinghe‐Arachchige

Wang

et al. 2022

J. Chem. Inf. Model.

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In this study, chemical promiscuity of a binuclear metallohydrolase Streptomyces griseus aminopeptidase (SgAP) has been investigated using DFT calculations. SgAP catalyzes two diverse reactions, peptide and phosphoester hydrolyses, using its binuclear (Zn–Zn) core. On the basis of the experimental information, mechanisms of these reactions have been investigated utilizing leucine p-nitro aniline (Leu-pNA) and bis(4-nitrophenyl) phosphate (BNPP) as the substrates. The computed barriers of 16.5 and 16.8 kcal/mol for the most plausible mechanisms proposed by the DFT calculations are in good agreement with the measured values of 13.9 and 18.3 kcal/mol for the Leu-pNA and BNPP hydrolyses, respectively. The former was found to occur through the transfer of two protons, while the latter with only one proton transfer. They are in line with the experimental observations. The cleavage of the peptide bond was the rate-determining process for the Leu-pNA hydrolysis. However, the creation of the nucleophile and its attack on the electrophile phosphorus atom was the rate-determining step for the BNPP hydrolysis. These calculations showed that the chemical nature of the substrate and its binding mode influence the nucleophilicity of the metal bound hydroxyl nucleophile. Additionally, the nucleophilicity was found to be critical for the Leu-pNA hydrolysis, whereas double Lewis acid activation was needed for the BNPP hydrolysis. That could be one of the reasons why peptide hydrolysis can be catalyzed by both mononuclear and binuclear metal cofactors containing hydrolases, while phosphoester hydrolysis is almost exclusively by binuclear metallohydrolases. These results will be helpful in the development of versatile catalysts for chemically distinct hydrolytic reactions.

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Ферментативные Реакции В Химикоэнзиматическом Синтезе Лекарственных Препаратов (Обзор)

Cited by 2 publications

References 0 publications

Effect of lipid-lowering activity of the natural original enzyme preparation in the experiment

Effect of lipid-lowering activity of the natural original enzyme preparation in the experiment

Promiscuous Catalytic Activity of a BinuclearMetallohydrolase: Peptide and Phosphoester Hydrolyses

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