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Literature summary extracted from

  • Vitali, T.; Maffioli, E.; Tedeschi, G.; 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 (2016), Arch. Biochem. Biophys., 593, 24-37.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
1.14.13.225 additional information expression of truncated forms lacking the C-terminal, LIM and/or calponin homology CH regions. The CH, LIM and C-terminal regions lead to an increase of KmNADPH. The C-terminus also determines an about 10fold decrease of kcat Homo sapiens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.14.13.225 0.019
-
 NADPH isolated monooxygenase-like domain, pH 7.0, 25°C Homo sapiens
1.14.13.225 0.03
-
 [F-actin]-L-methionine wild-type, pH 7.0, 25°C Homo sapiens
1.14.13.225 0.134
-
 NADPH truncated form comprising the MO and CH domains, pH 7.0, 25°C Homo sapiens
1.14.13.225 0.23
-
 NADPH truncated form comprising the MO, CH and LIM domains, pH 7.0, 25°C Homo sapiens
1.14.13.225 0.375
-
 NADPH wild-type, pH 7.0, 25°C Homo sapiens

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.14.13.225 cytoplasm
-
 Homo sapiens 5737
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.14.13.225 Zn2+ 1.6 mol per mol of protein Homo sapiens

Organism

EC Number Organism UniProt Comment Textmining
1.14.13.225 Homo sapiens Q8TDZ2
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.13.225 [F-actin]-L-methionine + NADPH + O2 + H+
-
 Homo sapiens [F-actin]-L-methionine-(R)-S-oxide + NADP+ + H2O only 2-3 residues are oxidized in each actin monomer. Several residues, including Met44 and Met47, are modified with similar probability ?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.14.13.225 0.28
-
 NADPH wild-type, pH 7.0, 25°C Homo sapiens
1.14.13.225 2.5
-
 NADPH truncated form comprising the MO and CH domains, pH 7.0, 25°C Homo sapiens
1.14.13.225 3.1
-
 NADPH isolated monooxygenase-like domain, pH 7.0, 25°C Homo sapiens
1.14.13.225 3.5
-
 NADPH truncated form comprising the MO, CH and LIM domains, pH 7.0, 25°C Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.13.225 FAD
-
 Homo sapiens

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
1.14.13.225 0.75
-
 NADPH wild-type, pH 7.0, 25°C Homo sapiens
1.14.13.225 15.3
-
 NADPH truncated form comprising the MO, CH and LIM domains, pH 7.0, 25°C Homo sapiens
1.14.13.225 18.5
-
 NADPH truncated form comprising the MO and CH domains, pH 7.0, 25°C Homo sapiens
1.14.13.225 163
-
 NADPH isolated monooxygenase-like domain, pH 7.0, 25°C Homo sapiens