Organism | UniProt | Comment | Textmining |
---|---|---|---|
Mus musculus | Q8BML1 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | the reductive half-reaction of the mical2 hydroxylase domain is stimulated by F-actin. In the absence of actin, NADPH reduces the flavin relatively slowly. Actin speeds that reaction significantly. The separate monooxygenase domain has the classic regulatory behavior of flavin-dependent aromatic hydroxylases (Class A monooxygenases) with slow reduction of the flavin when the substrate to be oxygenated is absent | Mus musculus | ? | - |
? | |
[F-actin]-L-methionine + NADPH + O2 + H+ | - |
Mus musculus | [F-actin]-L-methionine-(R)-S-oxide + NADP+ + H2O | - |
? |
Synonyms | Comment | Organism |
---|---|---|
MICAL-2 | - |
Mus musculus |
Mical2 | - |
Mus musculus |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NADH | strong preference for NADPH over NADH caused by a large difference in binding | Mus musculus | |
NADPH | strong preference for NADPH over NADH caused by a large difference in binding. Mical22 is specific for the proR hydride of NADPH, with a 4.8fold kinetic isotope effect | Mus musculus |