Lipid peroxidation affects catalytic properties of rat liver mitochondrial monoamine oxidases and their sensitivity to proteolysis

Медведев, А. Е.; Kirkel, A. Z.; Kamyshanskaya, N. S.; Gorkin, V. Z.

doi:10.1016/0020-711x(88)90309-6

Cited by 9 publications

(2 citation statements)

References 23 publications

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“…Residues at both entrances are closely associated with the membrane. Given the insight from these computational studies, new investigation of previously observed lipid effects on rat mitochondria MAO could provide further understanding of the importance in vivo [110][111][112][113][114]. Could alterations in the membrane composition (from diet, for example) have consequences for activity, raising or lowering the monoamine pool in the brain?…”

Section: The Influence Of the Membrane On Mao Activitymentioning

confidence: 99%

Questions in the Chemical Enzymology of MAO

Ramsay

Albreht

2021

Chemistry

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We have structure, a wealth of kinetic data, thousands of chemical ligands and clinical information for the effects of a range of drugs on monoamine oxidase activity in vivo. We have comparative information from various species and mutations on kinetics and effects of inhibition. Nevertheless, there are what seem like simple questions still to be answered. This article presents a brief summary of existing experimental evidence the background and poses questions that remain intriguing for chemists and biochemists researching the chemical enzymology of and drug design for monoamine oxidases (FAD-containing EC 4.1.3.4).

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Section: The Influence Of the Membrane On Mao Activitymentioning

confidence: 99%

Questions in the Chemical Enzymology of MAO

Ramsay

Albreht

2021

Chemistry

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“…The Gorkin's team found that oxidative modification of MAO (A) was accompanied by alteration in the substrate specificity of this enzyme and sensitivity to specific inhibitors [1][2][3]. The oxidized enzyme also exhibited increased sen sitivity to proteolytic enzymes [3][4][5]. Analysis of the 1 To whom correspondence should be addressed.…”

Section: Introductionmentioning

confidence: 99%

Computer modelling of monoamine oxidases

Veselovsky

Ivanov

Медведев

2015

Biochem. Moscow Suppl. Ser. B

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The article summarized results of long term studies on active site structures of monoamine oxi dase (MAO) performed in the Institute of Biomedical Chemistry (Russia) by computer modeling approaches. In mammals MAO exists in two highly homologous forms, MAO A and MAO B, distinguished by substrate specificity, inhibitor selectivity, and other characteristics. The development of approaches for active site mod eling of these enzymes (with unknown three dimensional structures) was originally based on analysis of inhibitory activity of selective inhibitors. It started from the analysis of relationships between the geometrical sizes of conformationally rigid molecules and their inhibitory activity. These studies resulted in molding of the active site structures of MAO A and MAO B. These molds reflect the sizes and shapes of active sites of these enzymes. These mold models have been used for virtual screening of molecular databases for new selec tive and non selective MAO inhibitors. The generated models have been compared with three dimensional structures of MAO A and MAO B, which appeared later.

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