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1.14.13.148: trimethylamine monooxygenase

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

Word Map on EC 1.14.13.148

Reaction

N,N,N-trimethylamine
+
NADPH
+
H+
+
O2
=
N,N,N-trimethylamine N-oxide
+
NADP+
+
H2O

Synonyms

dimethyl sulfoxide/trimethylamine N-oxide reductase, EC 1.14.13.8, FAD-containing monooxygenase, flavin containing monooxygenase 3, flavin monooxygenase 3, flavin-containing monooxygenase, flavin-containing monooxygenase 3, FMO, FMO3, FMO4, PB7211, TMA monooxygenase, TMA N-oxygenase, TMM

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
                1.14.13.148 trimethylamine monooxygenase

Engineering

Engineering on EC 1.14.13.148 - trimethylamine monooxygenase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D314A
mutation decreases the activity significantly
D314E
enzymatic activity and the apparent KM toward NADPH are only slightly affected
H227A
increase in apparent Km value
N288A
increase in apparent Km value
N72A
increase in apparent Km value
R226A
increase in apparent Km value
R409A
increase in apparent Km value
S203A
increase in apparent Km value
E158K
E24D
the mutation impacts the structure of the Rossmann fold involved in FAD binding and does not alter FMO3 catalytic activity
E305X
-
the mutation is associated with trimethylaminuria
E308G
K416N
the mutation has minimal impact on either hydrophilicity or protein structure
M66I
-
the mutation is associated with trimethylaminuria
N245N
-
the mutation is associated with trimethylaminuria
N61K
the mutation disrupts the secondary structure of a conserved membrane interaction domain and does not alter FMO3 catalytic activity
P153L
-
the mutation is associated with trimethylaminuria
P153L/E305X
-
the mutation is associated with trimethylaminuria
S310S
-
the mutation is associated with trimethylaminuria
T428R
-
methimazole activity of the mutant enzyme is stimulated (maximally 25% when the methimazole concentration is 2 mM) to the same extend of native enzyme up to an imipramine concentration of 3 mM. The activity of the mutant is inhibited at concentrations above 0.3 mM imipramine, 0.75 mM imipramine causes 93% inhibition of methimazole activity of the mutant enzyme. Chlorpromazine activates the mutant enzyme only at high substrate concentrations (0.1-2 mM)
V257M