Information on EC 1.14.13.239 - carnitine monooxygenase

for references in articles please use BRENDA:EC1.14.13.239
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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.14.13.239
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RECOMMENDED NAME
GeneOntology No.
carnitine monooxygenase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-carnitine + NAD(P)H + H+ + O2 = (3R)-3-hydroxy-4-oxobutanoate + trimethylamine + NAD(P)+ + H2O
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
L-carnitine degradation III
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SYSTEMATIC NAME
IUBMB Comments
L-carnitine,NAD(P)H:oxygen oxidoreductase (trimethylamine-forming)
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
alpha subunit and beta subunit
D0C9N6, D0C9N8
SwissProt
Manually annotated by BRENDA team
alpha subunit and beta subunit
D0C9N6, D0C9N8
SwissProt
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
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-
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Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
D-carnitine + NADH + H+ + O2
(3S)-3-hydroxy-4-oxobutanoate + trimethylamine + NAD+ + H2O
show the reaction diagram
D-carnitine + NADPH + H+ + O2
(3S)-3-hydroxy-4-oxobutanoate + trimethylamine + NADP+ + H2O
show the reaction diagram
L-carnitine + NADH + H+ + O2
(3R)-3-hydroxy-4-oxobutanoate + trimethylamine + NAD+ + H2O
show the reaction diagram
L-carnitine + NADPH + H+ + O2
(3R)-3-hydroxy-4-oxobutanoate + trimethylamine + NADP+ + H2O
show the reaction diagram
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
L-carnitine + NADH + H+ + O2
(3R)-3-hydroxy-4-oxobutanoate + trimethylamine + NAD+ + H2O
show the reaction diagram
L-carnitine + NADPH + H+ + O2
(3R)-3-hydroxy-4-oxobutanoate + trimethylamine + NADP+ + H2O
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
FAD
D0C9N6; D0C9N8;
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NAD+
D0C9N6; D0C9N8;
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NADPH
[2Fe-2S]-center
D0C9N6; D0C9N8;
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
His-tag affinity column chromatography
D0C9N6; D0C9N8;
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21pLysS cells
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expressed in Escherichia coli BLR(DE3) pLysS cells
D0C9N6; D0C9N8;
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E205A
D0C9N6; D0C9N8;
inactive
E205D
D0C9N6; D0C9N8;
inactive