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Literature summary for 1.14.13.239 extracted from

  • 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 (2020), J. Biol. Chem., 295, 13065-13078 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.14.13.239

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Acinetobacter baumannii

Protein Variants

Protein Variants Comment Organism
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 Acinetobacter baumannii
E205D mutation of the bridging Glu205 residue of subunit CntA, mutant shows no detectable enzymatic activity and a moderately reduced Fe and sulfur content Acinetobacter baumannii
E205Q mutation of the bridging Glu205 residue of subunit CntA, mutant shows no detectable enzymatic activity and a moderately reduced Fe and sulfur content Acinetobacter baumannii
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 Acinetobacter baumannii

Metals/Ions

Metals/Ions Comment Organism Structure
Iron subunit CntB carries a plant-type [2Fe-2S] cluster. CntA contains a [2Fe-2S] cluster and a mononuclear iron center Acinetobacter baumannii

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
139000
-
 gel filtration, subunit CntA Acinetobacter baumannii

Organism

Organism UniProt Comment Textmining
Acinetobacter baumannii D0C9N6 AND D0C9N8 D0C9N6 i.e. catalytic subunit CntA, D0C9N8 i.e. reductase subunit D0C9N8
-
Acinetobacter baumannii DSM 30007 D0C9N6 AND D0C9N8 D0C9N6 i.e. catalytic subunit CntA, D0C9N8 i.e. reductase subunit D0C9N8
-

Source Tissue

Source Tissue Comment Organism Textmining

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-carnitine + NADH + H+ + O2
-
 Acinetobacter baumannii (3R)-3-hydroxy-4-oxobutanoate + trimethylamine + NAD+ + H2O
-
 ?
L-carnitine + NADH + H+ + O2
-
 Acinetobacter baumannii DSM 30007 (3R)-3-hydroxy-4-oxobutanoate + trimethylamine + NAD+ + H2O
-
 ?

Subunits

Subunits Comment Organism
? 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 Acinetobacter baumannii

Synonyms

Synonyms Comment Organism
CntA
-
 Acinetobacter baumannii
CntB
-
 Acinetobacter baumannii

Cofactor

Cofactor Comment Organism Structure
FMN cofactor of subunit CntB Acinetobacter baumannii
[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 Acinetobacter baumannii

General Information

General Information Comment Organism
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 Acinetobacter baumannii