ExplorEnz: EC 1.14.13.225

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1.14.13.225

Accepted name:

F-actin monooxygenase

Reaction:

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

Other name(s):

MICAL (gene name)

Systematic name:

[F-actin]-L-methionine,NADPH:O₂ S-oxidoreductase

Comments:

The enzyme, characterized from the fruit fly Drosophila melanogaster, is a multi-domain oxidoreductase that acts as an F-actin disassembly factor. The enzyme selectively reduces two L-Met residues of F-actin, causing fragmentation of the filaments and preventing repolymerization [1]. Free methionine is not a substrate [2]. The reaction is stereospecific and generates the (R)-sulfoxide [3]. In the absence of substrate, the enzyme can act as an NAD(P)H oxidase (EC 1.6.3.1) [4,5].

Links to other databases:

BRENDA, EXPASY, KEGG, MetaCyc, PDB

References:

1.	Hung, R.J., Yazdani, U., Yoon, J., Wu, H., Yang, T., Gupta, N., Huang, Z., van Berkel, W.J. and Terman, J.R. Mical links semaphorins to F-actin disassembly. Nature 463 (2010) 823–827. [DOI] [PMID: 20148037]
2.	Hung, R.J., Pak, C.W. and Terman, J.R. Direct redox regulation of F-actin assembly and disassembly by Mical. Science 334 (2011) 1710–1713. [DOI] [PMID: 22116028]
3.	Hung, R.J., Spaeth, C.S., Yesilyurt, H.G. and Terman, J.R. SelR reverses Mical-mediated oxidation of actin to regulate F-actin dynamics. Nat. Cell Biol. 15 (2013) 1445–1454. [DOI] [PMID: 24212093]
4.	Zucchini, D., Caprini, G., Pasterkamp, R.J., Tedeschi, G. and Vanoni, M.A. Kinetic and spectroscopic characterization of the putative monooxygenase domain of human MICAL-1. Arch. Biochem. Biophys. 515 (2011) 1–13. [DOI] [PMID: 21864500]
5.	Vitali, T., Maffioli, E., Tedeschi, G. and Vanoni, M.A. Properties and catalytic activities of MICAL1, the flavoenzyme involved in cytoskeleton dynamics, and modulation by its CH, LIM and C-terminal domains. Arch. Biochem. Biophys. 593 (2016) 24–37. [DOI] [PMID: 26845023]

[EC 1.14.13.225 created 2016]