MICAL1 produces NADP+, H2O2

Stable Identifier
R-HSA-8865107
Type
Reaction [omitted]
Species
Homo sapiens
Compartment
ReviewStatus
5/5
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MICAL1 is involved in cytoskeleton dynamics through its NADPH-dependent oxidase and F-actin depolymerizing activities. MICAL1 inhibits actin polymerization and promotes actin depolymerization (Hung et al. 2011). F-actin is thought to bind and stabilize the flavoprotein domain in MICAL's active conformation (Kolk & Pasterkamp 2007). Actin depolymerization mediated by MICAL1 is thought to be a consequence of H2O2 produced by MICAL1 NADPH oxidase activity (Nadella et al. 2005, Zucchini et al. 2011), rather than due to direct hydroxylation of actin methionine residues (Vitali et al. 2016).
Literature References
PubMed ID Title Journal Year
26845023 Properties and catalytic activities of MICAL1, the flavoenzyme involved in cytoskeleton dynamics, and modulation by its CH, LIM and C-terminal domains

Maffioli, E, Tedeschi, G, Vitali, T, Vanoni, MA

Arch. Biochem. Biophys. 2016
Participants
Participates
Catalyst Activity

monooxygenase activity of MICAL1:FAD [cytosol]

Orthologous Events
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