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1-butyl-trimethylammonium + NADH + H+ + O2
? + trimethylamine + NAD+ + H2O
-
-
-
?
D-carnitine + NADH + H+ + O2
(3S)-3-hydroxy-4-oxobutanoate + 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 + NADH + H+ + O2
(3R)-3-hydroxy-4-oxobutanoate + 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
-
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
-
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
-
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
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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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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 + 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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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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?

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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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
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

inactive
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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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