methylputrescine oxidase activity

Definition

Target type: molecularfunction

Catalysis of the reaction: N-methylputrescine + H2O + O2 = N-methylaminobutanal + NH3 + hydrogen peroxide + H+. [MetaCyc:RXN-8244, PMID:17283012, PMID:24287136]

Methylputrescine oxidase activity is a crucial enzyme involved in the polyamine catabolism pathway, specifically in the degradation of polyamines such as spermidine and spermine. This enzyme catalyzes the oxidation of methylputrescine, a derivative of the polyamine putrescine, to 4-aminobutanal. The reaction involves the removal of two electrons and two protons from the substrate, resulting in the formation of a carbonyl group. This oxidative deamination reaction is essential for the regulation of polyamine levels in cells. Methylputrescine oxidase is a flavin-containing enzyme, with FAD serving as a cofactor. It is located in the mitochondrial matrix and has a broad substrate specificity, acting on various polyamine analogs. The precise mechanism of action involves the binding of methylputrescine to the active site of the enzyme, followed by the transfer of electrons from the substrate to the FAD cofactor. This redox reaction is coupled to the reduction of molecular oxygen to water. The resulting 4-aminobutanal product can then be further metabolized by other enzymes in the polyamine degradation pathway. This enzyme plays a vital role in maintaining cellular homeostasis by regulating polyamine levels, which are crucial for various cellular processes, including cell growth, proliferation, and differentiation. Dysregulation of methylputrescine oxidase activity has been implicated in various diseases, including cancer and neurodegenerative disorders.'
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Proteins (1)

Compounds (3)