Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.14.13.239 extracted from

  • 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 (2021), J. Biol. Chem., 296, 100038 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.14.13.239

Crystallization (Commentary)

Crystallization (Comment) Organism
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 Acinetobacter baumannii

Protein Variants

Protein Variants Comment Organism
Y203F mutant is active Acinetobacter baumannii

Inhibitors

Inhibitors Comment Organism Structure
6-(5-bromopyridin-3-yl)-N-[3-(1H-imidazol-1-yl)propyl]-2-phenylpyrimidin-4-amine
-
 Acinetobacter baumannii
N-[(oxan-4-yl)methyl]-5-(thiophen-2-yl)imidazo[2,1-b][1,3,4]thiadiazol-2-amine
-
 Acinetobacter baumannii
N-[3-(1H-imidazol-1-yl)propyl]-8-methyl-1,6-naphthyridine-2-carboxamide
-
 Acinetobacter baumannii

Metals/Ions

Metals/Ions Comment Organism Structure
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 Acinetobacter baumannii

Organism

Organism UniProt Comment Textmining
Acinetobacter baumannii A0A059ZPP5 oxygenase subunit CntA
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1-butyl-trimethylammonium + NADH + H+ + O2
-
 Acinetobacter baumannii ? + trimethylamine + NAD+ + H2O
-
 ?
gamma-butyrobetaine + NADH + H+ + O2
-
 Acinetobacter baumannii ? + trimethylamine + NAD+ + H2O
-
 ?
L-carnitine + NADH + H+ + O2
-
 Acinetobacter baumannii (3R)-3-hydroxy-4-oxobutanoate + trimethylamine + NAD+ + H2O
-
 ?
meldonium + NADH + H+ + O2
-
 Acinetobacter baumannii ? + trimethylamine + NAD+ + H2O
-
 ?
additional information substrates with longer alkyl chains, e.g. hexyl, or other functional groups show no activity Acinetobacter baumannii ?
-
-

Synonyms

Synonyms Comment Organism
CntA
-
 Acinetobacter baumannii

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
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 Acinetobacter baumannii

IC50 Value

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
0.0011
-
 pH 7.6, temperature not specified in the publication Acinetobacter baumannii 6-(5-bromopyridin-3-yl)-N-[3-(1H-imidazol-1-yl)propyl]-2-phenylpyrimidin-4-amine
0.0049
-
 pH 7.6, temperature not specified in the publication Acinetobacter baumannii N-[3-(1H-imidazol-1-yl)propyl]-8-methyl-1,6-naphthyridine-2-carboxamide
0.0058
-
 pH 7.6, temperature not specified in the publication Acinetobacter baumannii N-[(oxan-4-yl)methyl]-5-(thiophen-2-yl)imidazo[2,1-b][1,3,4]thiadiazol-2-amine