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Literature summary for 1.14.13.225 extracted from

  • Alqassim, S.S.; Urquiza, M.; Borgnia, E.; Nagib, M.; Amzel, L.M.; Bianchet, M.A.
    Modulation of MICAL monooxygenase activity by its calponin homology domain: structural and mechanistic insights (2016), Sci. Rep., 6, 22176.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
structure of a fragment of MICAL-1 containing the monooxygenase and the calponin homology domains. The calponin homology domain, loosely connected to the monooxygenase domain by a flexible linker and is far away from the catalytic site, couples F-actin to the enhancement of redox activity of MICALMO-CH by a cooperative mechanism involving a trans interaction between adjacently bound molecules Mus musculus

Organism

Organism UniProt Comment Textmining
Mus musculus Q8VDP3
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-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
[F-actin]-L-methionine + NADPH + O2 + H+
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Mus musculus [F-actin]-L-methionine-(R)-S-oxide + NADP+ + H2O
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?

Synonyms

Synonyms Comment Organism
MICAL1
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Mus musculus