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1.14.13.225: F-actin monooxygenase

This is an abbreviated version!
For detailed information about F-actin monooxygenase, go to the full flat file.

Word Map on EC 1.14.13.225

Reaction

[F-actin]-L-methionine
+
NADPH
+
O2
+
H+
=
[F-actin]-L-methionine-(R)-S-oxide
+
NADP+
+
H2O

Synonyms

MICAL, MICAL-1, MICAL-2, MICAL1, Mical2, MICAL2PV, MICAL3

ECTree

     1 Oxidoreductases
         1.14 Acting on paired donors, with incorporation or reduction of molecular oxygen
             1.14.13 With NADH or NADPH as one donor, and incorporation of one atom of oxygen into the other donor
                1.14.13.225 F-actin monooxygenase

Crystallization

Crystallization on EC 1.14.13.225 - F-actin monooxygenase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
MICAL3 has an FAD/NADP-binding Rossmann-fold domain for monooxygenase activity. The flavin-containing monooxygenase (FMO) and calponin-homology (CH) domains of both MICAL3 and MICAL1 are highly similar in structure, but a different relative position of the calponin-homology domain in the asymmetric unit
purified recombinant His-tagged wild-type and mutant MICAL3 variants, sitting drop vapor diffusion method, method optimization, mixing of 500 nl of 25 mg/ml protein in 50 mM Tris, pH 8.5, 100 mM NaCl, 1 mM 1,4-dithiothreitol, 1% glycerol, with 500 nl of crystallization solution containing 0.1 M bicine-NaOH, pH 9.2, 7% v/v MPD, one day, X-ray diffraction structure determination and analysis at 1.9-2.3 A resolution
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