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Information on EC 1.14.13.148 - trimethylamine monooxygenase and Organism(s) Oryctolagus cuniculus and UniProt Accession P32417

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IUBMB Comments
A flavoprotein. The bacterial enzyme enables bacteria to use trimethylamine as the sole source of carbon and energy [1,4]. The mammalian enzyme is involved in detoxification of trimethylamine. Mutations in the human enzyme cause the inheritable disease known as trimethylaminuria (fish odor syndrome) [2,3].
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Oryctolagus cuniculus
UNIPROT: P32417
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The taxonomic range for the selected organisms is: Oryctolagus cuniculus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
flavin monooxygenase 3, trimethylamine monooxygenase, tma monooxygenase, tma n-oxygenase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
EC 1.14.13.8
assigned to
flavin-containing monooxygenase
-
EC 1.14.13.8
assigned to
flavin-containing monooxygenase
-
SYSTEMATIC NAME
IUBMB Comments
N,N,N-trimethylamine,NADPH:oxygen oxidoreductase (N-oxide-forming)
A flavoprotein. The bacterial enzyme enables bacteria to use trimethylamine as the sole source of carbon and energy [1,4]. The mammalian enzyme is involved in detoxification of trimethylamine. Mutations in the human enzyme cause the inheritable disease known as trimethylaminuria (fish odor syndrome) [2,3].
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
methimazole + NADPH + H+ + O2
methimazole N-oxide + NADP+ + H2O
show the reaction diagram
-
-
-
?
methimazole + NADPH + H+ + O2
methimazole N-oxide + NADP+ + H2O
show the reaction diagram
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
NADPH
required for activity
NADPH
required for activity
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.03
Methimazole
isoform FMO3, at pH 8.4, temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.025
isoform FMO3, using 1 mM methimazole as substrate, at pH 8.4, temperature not specified in the publication
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isoform FMO3
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
isoform FMO3 is most prominent in the liver
Manually annotated by BRENDA team
isoform FMO4 is most prominent in the kidney
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
FMO3_RABIT
531
1
59815
Swiss-Prot
other Location (Reliability: 3)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
59815
59815, isofom FMO3, calculated from amino acid sequence
62992
x * 62992, isoform FMO4, calculated from amino acid sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
59815, isofom FMO3, calculated from amino acid sequence
?
x * 62992, isoform FMO4, calculated from amino acid sequence
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Saccharomyces cerevisiae strain 334 and in Escherichia coli JM109 cells
expressed in Saccharomyces cerevisiae strain 334 and in Escherichia coli JM109 cells
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Burnettt, V.; Lawton, M.; Philpot, R.
Cloning and sequencing of flavin-containing monooxygenases FMO3 and FMO4 from rabbit and characterization of FMO3
J. Biol. Chem.
269
14314-14322
1994
Oryctolagus cuniculus (P32417), Oryctolagus cuniculus (P36367)
Manually annotated by BRENDA team