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Information on EC 1.14.13.239 - carnitine monooxygenase
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EC Tree
1.14.13.239 carnitine monooxygenaseIUBMB Comments
The bacterial enzyme is a complex consisting of a reductase and an oxygenase components. The reductase subunit contains a flavin and a plant-type ferredoxin [2Fe-2S] cluster, while the oxygenase subunit is a Rieske-type protein in which a [2Fe-2S] cluster is coordinated by two histidine and two cysteine residues.
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Word Map
- 1.14.13.239
-
surfactant
- bromide
-
tension
-
micelle
-
alkyltrimethylammonium
-
interfacial
- alkane
-
air-water
-
reorientation
-
rieske
-
foam
-
flocculation
-
rieske-type
-
co-adsorption
-
langmuir
-
n-alkyl
-
fluorocarbon
- trimethylamine-n-oxide
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
Synonyms
cntab, carnitine monooxygenase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
carnitine TMA lyase
CntA
cntAB
CntB
yeaWX
cntAB
-
-
-
-
yeaWX
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-carnitine + NAD(P)H + H+ + O2 = (3R)-3-hydroxy-4-oxobutanoate + trimethylamine + NAD(P)+ + H2O
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
-
-
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SYSTEMATIC NAME
IUBMB Comments
L-carnitine,NAD(P)H:oxygen oxidoreductase (trimethylamine-forming)
The bacterial enzyme is a complex consisting of a reductase and an oxygenase components. The reductase subunit contains a flavin and a plant-type ferredoxin [2Fe-2S] cluster, while the oxygenase subunit is a Rieske-type protein in which a [2Fe-2S] cluster is coordinated by two histidine and two cysteine residues.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1-butyl-trimethylammonium + NADH + H+ + O2
? + trimethylamine + NAD+ + H2O
-
-
-
?
D-carnitine + NADPH + H+ + O2
(3S)-3-hydroxy-4-oxobutanoate + trimethylamine + NADP+ + H2O
gamma-butyrobetaine + NADH + H+ + O2
? + trimethylamine + NAD+ + H2O
-
-
-
?
L-carnitine + NADPH + H+ + O2
(3R)-3-hydroxy-4-oxobutanoate + trimethylamine + NADP+ + H2O
meldonium + NADH + H+ + O2
? + trimethylamine + NAD+ + H2O
-
-
-
?
additional information
?
-
substrates with longer alkyl chains, e.g. hexyl, or other functional groups show no activity
-
-
-
D-carnitine + NADH + H+ + O2
(3S)-3-hydroxy-4-oxobutanoate + trimethylamine + NAD+ + H2O
-
the enzyme shows higher activity with D-carnitine compared to L-carnitine
-
-
?
D-carnitine + NADH + H+ + O2
(3S)-3-hydroxy-4-oxobutanoate + trimethylamine + NAD+ + H2O
Acinetobacter calcoaceticus ATCC 39647
-
the enzyme shows higher activity with D-carnitine compared to L-carnitine
-
-
?
D-carnitine + NADH + H+ + O2
(3S)-3-hydroxy-4-oxobutanoate + trimethylamine + NAD+ + H2O
Acinetobacter calcoaceticus ATCC 39648
-
the enzyme shows higher activity with D-carnitine compared to L-carnitine
-
-
?
D-carnitine + NADPH + H+ + O2
(3S)-3-hydroxy-4-oxobutanoate + trimethylamine + NADP+ + H2O
-
the enzyme shows higher activity with D-carnitine compared to L-carnitine
-
-
?
D-carnitine + NADPH + H+ + O2
(3S)-3-hydroxy-4-oxobutanoate + trimethylamine + NADP+ + H2O
Acinetobacter calcoaceticus ATCC 39647
-
the enzyme shows higher activity with D-carnitine compared to L-carnitine
-
-
?
D-carnitine + NADPH + H+ + O2
(3S)-3-hydroxy-4-oxobutanoate + trimethylamine + NADP+ + H2O
Acinetobacter calcoaceticus ATCC 39648
-
the enzyme shows higher activity with D-carnitine compared to L-carnitine
-
-
?
L-carnitine + NADH + H+ + O2
(3R)-3-hydroxy-4-oxobutanoate + trimethylamine + NAD+ + H2O
-
-
-
?
L-carnitine + NADH + H+ + O2
(3R)-3-hydroxy-4-oxobutanoate + trimethylamine + NAD+ + H2O
-
-
-
-
?
L-carnitine + NADH + H+ + O2
(3R)-3-hydroxy-4-oxobutanoate + trimethylamine + NAD+ + H2O
-
-
-
?
L-carnitine + NADH + H+ + O2
(3R)-3-hydroxy-4-oxobutanoate + trimethylamine + NAD+ + H2O
-
-
-
?
L-carnitine + NADH + H+ + O2
(3R)-3-hydroxy-4-oxobutanoate + trimethylamine + NAD+ + H2O
-
-
-
?
L-carnitine + NADH + H+ + O2
(3R)-3-hydroxy-4-oxobutanoate + trimethylamine + NAD+ + H2O
-
-
-
-
?
L-carnitine + NADH + H+ + O2
(3R)-3-hydroxy-4-oxobutanoate + trimethylamine + NAD+ + H2O
Acinetobacter calcoaceticus ATCC 39647
-
-
-
-
?
L-carnitine + NADH + H+ + O2
(3R)-3-hydroxy-4-oxobutanoate + trimethylamine + NAD+ + H2O
Acinetobacter calcoaceticus ATCC 39648
-
-
-
-
?
L-carnitine + NADH + H+ + O2
(3R)-3-hydroxy-4-oxobutanoate + trimethylamine + NAD+ + H2O
-
-
-
-
?
L-carnitine + NADH + H+ + O2
(3R)-3-hydroxy-4-oxobutanoate + trimethylamine + NAD+ + H2O
-
-
-
-
?
L-carnitine + NADPH + H+ + O2
(3R)-3-hydroxy-4-oxobutanoate + trimethylamine + NADP+ + H2O
-
-
-
?
L-carnitine + NADPH + H+ + O2
(3R)-3-hydroxy-4-oxobutanoate + trimethylamine + NADP+ + H2O
-
-
-
?
L-carnitine + NADPH + H+ + O2
(3R)-3-hydroxy-4-oxobutanoate + trimethylamine + NADP+ + H2O
-
-
-
-
?
L-carnitine + NADPH + H+ + O2
(3R)-3-hydroxy-4-oxobutanoate + trimethylamine + NADP+ + H2O
Acinetobacter calcoaceticus ATCC 39647
-
-
-
-
?
L-carnitine + NADPH + H+ + O2
(3R)-3-hydroxy-4-oxobutanoate + trimethylamine + NADP+ + H2O
Acinetobacter calcoaceticus ATCC 39648
-
-
-
-
?
L-carnitine + NADPH + H+ + O2
(3R)-3-hydroxy-4-oxobutanoate + trimethylamine + NADP+ + H2O
-
-
-
-
?
L-carnitine + NADPH + H+ + O2
(3R)-3-hydroxy-4-oxobutanoate + trimethylamine + NADP+ + H2O
-
-
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-carnitine + NADPH + H+ + O2
(3R)-3-hydroxy-4-oxobutanoate + trimethylamine + NADP+ + H2O
L-carnitine + NADH + H+ + O2
(3R)-3-hydroxy-4-oxobutanoate + trimethylamine + NAD+ + H2O
-
-
-
?
L-carnitine + NADH + H+ + O2
(3R)-3-hydroxy-4-oxobutanoate + trimethylamine + NAD+ + H2O
-
-
-
?
L-carnitine + NADH + H+ + O2
(3R)-3-hydroxy-4-oxobutanoate + trimethylamine + NAD+ + H2O
-
-
-
-
?
L-carnitine + NADH + H+ + O2
(3R)-3-hydroxy-4-oxobutanoate + trimethylamine + NAD+ + H2O
-
-
-
-
?
L-carnitine + NADPH + H+ + O2
(3R)-3-hydroxy-4-oxobutanoate + trimethylamine + NADP+ + H2O
-
-
-
?
L-carnitine + NADPH + H+ + O2
(3R)-3-hydroxy-4-oxobutanoate + trimethylamine + NADP+ + H2O
-
-
-
?
L-carnitine + NADPH + H+ + O2
(3R)-3-hydroxy-4-oxobutanoate + trimethylamine + NADP+ + H2O
-
-
-
-
?
L-carnitine + NADPH + H+ + O2
(3R)-3-hydroxy-4-oxobutanoate + trimethylamine + NADP+ + H2O
-
-
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
[2Fe-2S]-center
subunit CntB carries a plant-type [2Fe-2S] cluster. CntA contains a [2Fe-2S] cluster and a mononuclear iron center. Hierarchical metallocenter maturation of Rieske [2Fe-2S] is followed by the mononuclear [Fe]center
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Iron
Iron
subunit CntB carries a plant-type [2Fe-2S] cluster. CntA contains a [2Fe-2S] cluster and a mononuclear iron center
Iron
the mononuclear Fe exists in an octahedral geometry and is coordinated by two histidine ligands (His213, His208) and a bidentate aspartate residue (Asp 323) in a His-His-Asp catalytic triad
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
6-(5-bromopyridin-3-yl)-N-[3-(1H-imidazol-1-yl)propyl]-2-phenylpyrimidin-4-amine
-
-
N-[(oxan-4-yl)methyl]-5-(thiophen-2-yl)imidazo[2,1-b][1,3,4]thiadiazol-2-amine
-
-
N-[3-(1H-imidazol-1-yl)propyl]-8-methyl-1,6-naphthyridine-2-carboxamide
-
-
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0011
N-[3-(1H-imidazol-1-yl)propyl]-8-methyl-1,6-naphthyridine-2-carboxamide
pH 7.6, temperature not specified in the publication
-
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0011
6-(5-bromopyridin-3-yl)-N-[3-(1H-imidazol-1-yl)propyl]-2-phenylpyrimidin-4-amine
Acinetobacter baumannii
pH 7.6, temperature not specified in the publication
-
0.0058
N-[(oxan-4-yl)methyl]-5-(thiophen-2-yl)imidazo[2,1-b][1,3,4]thiadiazol-2-amine
Acinetobacter baumannii
pH 7.6, temperature not specified in the publication
-
0.0049
N-[3-(1H-imidazol-1-yl)propyl]-8-methyl-1,6-naphthyridine-2-carboxamide
Acinetobacter baumannii
pH 7.6, temperature not specified in the publication
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
alpha subunit and beta subunit
SwissProt
brenda
D0C9N6 i.e. catalytic subunit CntA, D0C9N8 i.e. reductase subunit D0C9N8
SwissProt
brenda
D0C9N6 i.e. catalytic subunit CntA, D0C9N8 i.e. reductase subunit D0C9N8
SwissProt
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
physiological function
during NADH-dependent electron transfer via the redox components of CntB and within the trimeric CntA complex, the two electrons from NADH are allocated to the plant-type [2Fe-2S] cluster and to FMN as a flavin semiquinone radical. The translocation of the first electron occurs onto the [Fe] center and the second electron onto the Rieske-type [2Fe-2S] cluster of CntA to finally allow for oxygen activation as a basis for carnitine cleavage. An unusual intermolecular electron transfer takes place between the subunits of the CntA trimer via the bridging residue Glu-205
physiological function
-
during NADH-dependent electron transfer via the redox components of CntB and within the trimeric CntA complex, the two electrons from NADH are allocated to the plant-type [2Fe-2S] cluster and to FMN as a flavin semiquinone radical. The translocation of the first electron occurs onto the [Fe] center and the second electron onto the Rieske-type [2Fe-2S] cluster of CntA to finally allow for oxygen activation as a basis for carnitine cleavage. An unusual intermolecular electron transfer takes place between the subunits of the CntA trimer via the bridging residue Glu-205
-
Show AA Sequence and Transmembrane Helices (1495 entries)
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Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
x * 45000, SDS-PAGE, x * 37151, calculated from sequence, recombinant His-tagged subunit CntB. 3 * 43000, SDS-PAGE, 3 * 43155, calculated from sequence, recombinant subunit CntA. CntA is a functional trimer
?
-
x * 45000, SDS-PAGE, x * 37151, calculated from sequence, recombinant His-tagged subunit CntB. 3 * 43000, SDS-PAGE, 3 * 43155, calculated from sequence, recombinant subunit CntA. CntA is a functional trimer
-
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
structures of the oxygenase subunit CntA. CntA exists in a head-to-tail alpha3 trimeric structure. The Rieske and the catalytic mononuclear iron domains are located more than 40 A apart in the same monomer but adjacent in two neighboring monomers. Tyrosine residue Y203 is essential for ligand recognition through a pi-cation interaction with the quaternary ammonium group
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D75K
mutation in putative FMN-binding residue of subunit CntB, mutant reveals a characteristic decrease of the absorption at 340 and 463 nm and the parallel reduction of the fluorescence signal at 526 nm plus a significant decrease of the cofactor content. 70% residual activity
E205D
E205Q
mutation of the bridging Glu205 residue of subunit CntA, mutant shows no detectable enzymatic activity and a moderately reduced Fe and sulfur content
S82A
mutation in putative FMN-binding residue of subunit CntB, mutant reveals a characteristic decrease of the absorption at 340 and 463 nm and the parallel reduction of the fluorescence signal at 526 nm plus a significant decrease of the cofactor content. 35% residual activity
D75K
-
mutation in putative FMN-binding residue of subunit CntB, mutant reveals a characteristic decrease of the absorption at 340 and 463 nm and the parallel reduction of the fluorescence signal at 526 nm plus a significant decrease of the cofactor content. 70% residual activity
-
E205D
-
mutation of the bridging Glu205 residue of subunit CntA, mutant shows no detectable enzymatic activity and a moderately reduced Fe and sulfur content
-
E205Q
-
mutation of the bridging Glu205 residue of subunit CntA, mutant shows no detectable enzymatic activity and a moderately reduced Fe and sulfur content
-
S82A
-
mutation in putative FMN-binding residue of subunit CntB, mutant reveals a characteristic decrease of the absorption at 340 and 463 nm and the parallel reduction of the fluorescence signal at 526 nm plus a significant decrease of the cofactor content. 35% residual activity
-
E205D
mutation of the bridging Glu205 residue of subunit CntA, mutant shows no detectable enzymatic activity and a moderately reduced Fe and sulfur content
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ditullio, D.; Anderson, D.; Chen, C.S.; Sih, C.J.
L-carnitine via enzyme-catalyzed oxidative kinetic resolution
Bioorg. Med. Chem.
2
415-420
1994
Acinetobacter calcoaceticus, Acinetobacter calcoaceticus ATCC 39648, Acinetobacter calcoaceticus ATCC 39647
brenda
Koeth, R.; Levison, B.; Culley, M.; Buffa, J.; Wang, Z.; Gregory, J.; Org, E.; Wu, Y.; Li, L.; Smith, J.; Tang, W.; Didonato, J.; Lusis, A.; Hazen, S.
gamma-Butyrobetaine is a proatherogenic intermediate in gut microbial metabolism of L-carnitine to TMAO
Cell Metab.
20
799-812
2014
Escherichia coli, Escherichia coli DH10B
brenda
Zhu, Y.; Jameson, E.; Crosatti, M.; Schaefer, H.; Rajakumar, K.; Bugg, T.D.; Chen, Y.
Carnitine metabolism to trimethylamine by an unusual Rieske-type oxygenase from human microbiota
Proc. Natl. Acad. Sci. USA
111
4268-4273
2014
Acinetobacter baumannii (D0C9N6 AND D0C9N8), Acinetobacter baumannii, Acinetobacter baumannii ATCC19606 (D0C9N6 AND D0C9N8)
brenda
Massmig, M.; Reijerse, E.; Krausze, J.; Laurich, C.; Lubitz, W.; Jahn, D.; Moser, J.
Carnitine metabolism in the human gut characterization of the two-component carnitine monooxygenase CntAB from Acinetobacter baumannii
J. Biol. Chem.
295
13065-13078
2020
Acinetobacter baumannii (D0C9N6 AND D0C9N8), Acinetobacter baumannii, Acinetobacter baumannii DSM 30007 (D0C9N6 AND D0C9N8)
brenda
Quareshy, M.; Shanmugam, M.; Townsend, E.; Jameson, E.; Bugg, T.; Cameron, A.; Chen, Y.
Structural basis of carnitine monooxygenase CntA substrate specificity, inhibition, and intersubunit electron transfer
J. Biol. Chem.
296
100038
2021
Acinetobacter baumannii (A0A059ZPP5)
brenda
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