| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 8291440 | Archives of Biochemistry and Biophysics | 2011 | 13 Pages |
Abstract
⺠Human MICAL monooxygenase-like domain (MICAL-MO) was overproduced and purified. ⺠Results highlight the functional similarity with the p-hydroxybenzoate hydroxylase class. ⺠The NADPH-dependent actin depolymerizing activity of MICAL-MO is confirmed. ⺠F-actin enhances NAD(P)H oxidation by increasing both kcat and kcat/KNAD(P)H. ⺠The kinetics show that the effect of MICAL-MO on F-actin may be reversible.
Related Topics
Life Sciences
Biochemistry, Genetics and Molecular Biology
Biochemistry
Authors
Daniela Zucchini, Gianluca Caprini, R. Jeroen Pasterkamp, Gabriella Tedeschi, Maria A. Vanoni,