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[Oxidative modification of monoamine oxidase]
1Institute of Biomedical Chemistry, Moscow, Russia.
Abstract:
Oxidative modification of monoamine oxidases (MAO) accompanied by alteration of their substrate specificity and sensitivity to specific inhibitors was discovered by Professor V.Z. Gorkin more than 30 years ago. The mechanism of this phenomenon includes oxidation of SH groups of the enzyme. Oxidative modification of MAO is also accompanied by increased sensitivity to limited proreolysis. Modification of MAO was found in many pathological states, however, elucidation of biological role of this phenomenon requires further investigations.
Insights
Oxidative modification of monoamine oxidases (MAO) alters enzyme function and inhibitor sensitivity. This modification, involving SH group oxidation, is observed in various diseases, but its biological role needs further study.
Area of Science:
- Biochemistry
- Enzymology
Context:
- Monoamine oxidases (MAO) play crucial roles in neurotransmitter metabolism.
- Oxidative modification of MAO has been recognized for over 30 years.
Purpose:
- To summarize the phenomenon of oxidative modification of MAO.
- To highlight the mechanistic aspects and implications of MAO modification.
Summary:
- Oxidative modification of MAO leads to changes in substrate specificity and inhibitor sensitivity.
- The mechanism involves the oxidation of enzyme sulfhydryl (SH) groups.
- This modification also increases susceptibility to limited proteolysis.
Impact:
- MAO modification is observed in numerous pathological conditions.
- Further research is needed to fully elucidate the biological significance of MAO oxidative modification.
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