Information on EC 1.14.13.225 - F-actin monooxygenase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.14.13.225
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RECOMMENDED NAME
GeneOntology No.
F-actin monooxygenase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
[F-actin]-L-methionine + NADPH + O2 + H+ = [F-actin]-L-methionine-(R)-S-oxide + NADP+ + H2O
show the reaction diagram
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SYSTEMATIC NAME
IUBMB Comments
[F-actin]-L-methionine,NADPH:O2 S-oxidoreductase
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].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
[F-actin]-L-methionine + NADH + O2 + H+
[F-actin]-L-methionine-(R)-S-oxide + NAP+ + H2O
show the reaction diagram
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?
[F-actin]-L-methionine + NADPH + O2 + H+
[F-actin]-L-methionine-(R)-S-oxide + NADP+ + H2O
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
[F-actin]-L-methionine + NADPH + O2 + H+
[F-actin]-L-methionine-(R)-S-oxide + NADP+ + H2O
show the reaction diagram
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Mical post-translationally oxidizes the methionine 44 residue within the D-loop of actin, simultaneously severing filaments and decreasing polymerization
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADPH
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Zn2+
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1.6 mol per mol of protein
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
glycerol
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10%, 2fold increase in Km for NADPH
NaCl
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0.1 M, 20fold increase in Km for NADPH
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
cofilin
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cofilin enhances Mical-mediated actin filament disassembly. Mical and cofilin synergize to drive Semaphorin-Plexin repulsive signalling and axon guidance
F-actin
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.58
NADH
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pH 7.0, 25°C
0.019 - 0.499
NADPH
0.03
[F-actin]-L-methionine
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wild-type, pH 7.0, 25°C
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additional information
NADPH
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the Km for NADPH of the NADPH oxidase reaction is sensitive to ionic strength and type of ions. pH 7.0, 25°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.28
NADH
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pH 7.0, 25°C
0.28 - 4
NADPH
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.48
NADH
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pH 7.0, 25°C
0.75 - 163
NADPH
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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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