2-Aminobenzoyl-CoA monooxygenase/reductase, a novel type of flavoenzyme : studies on the stoichiometry and the course of the reaction

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1989
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Buder, Reiner
Ziegler, Klaus
Fuchs, Georg
Langkau, Bernd
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European Journal of Biochemistry ; 185 (1989), 3. - pp. 637-643. - ISSN 0014-2956. - eISSN 1432-1033
Abstract
The reaction catalyzed by 2-aminobenzoyl-coenzyme-A monooxygenase/reductase from a denitrifying Pseudomonas sp. has been investigated. 2-Aminobenzoyl-CoA and 2-amino[carboxy-14C]benzoyl-CoA were synthesized enzymatically using 2-aminobenzoyl-CoA synthetase from the same organism. The product was purified by chromatography and characterized by ultraviolet/visible and 1H-NMR spectroscopy. The conversion of 2-aminobenzoyl-CoA catalyzed by the monooxygenase/reductase requires NADH and oxygen, and yields at least two different products depending on the relative concentration of NADH. At [NADH]< Km (40 μM), i.e. [NADH]/[2-aminobenzoyl-CoA] ~ 0.02 0.05, the main product is probably a hydroxylated derivative of 2-aminobenzoyl-CoA, which is characterized by an absorbance maximum around 375 nm. When [NADH]/[2-aminobenzoyl-CoA] ~ 2 5, the predominant product is a non-aromatic coenzyme A thioester (λmax ~ 320 nm). The stoichiometry in this case is 2.1 2.4 mol NADH oxidized (mol oxygen consumed)−1 (mol 2-aminobenzoyl-CoA metabolized)−1. The product is extremely unstable in the acidic pH range and undergoes decarboxylation in a few minutes at pH < 5. Some degree of stabilisation is obtained upon reduction with sodium borohydride, probably resulting in a further reduced non-aromatic coenzyme-A thioester.
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ISO 690BUDER, Reiner, Klaus ZIEGLER, Georg FUCHS, Bernd LANGKAU, Sandro GHISLA, 1989. 2-Aminobenzoyl-CoA monooxygenase/reductase, a novel type of flavoenzyme : studies on the stoichiometry and the course of the reaction. In: European Journal of Biochemistry. 185(3), pp. 637-643. ISSN 0014-2956. eISSN 1432-1033. Available under: doi: 10.1111/j.1432-1033.1989.tb15160.x
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@article{Buder19892Amin-8209,
  year={1989},
  doi={10.1111/j.1432-1033.1989.tb15160.x},
  title={2-Aminobenzoyl-CoA monooxygenase/reductase, a novel type of flavoenzyme : studies on the stoichiometry and the course of the reaction},
  number={3},
  volume={185},
  issn={0014-2956},
  journal={European Journal of Biochemistry},
  pages={637--643},
  author={Buder, Reiner and Ziegler, Klaus and Fuchs, Georg and Langkau, Bernd and Ghisla, Sandro}
}
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    <dcterms:abstract xml:lang="eng">The reaction catalyzed by 2-aminobenzoyl-coenzyme-A monooxygenase/reductase from a denitrifying Pseudomonas sp. has been investigated. 2-Aminobenzoyl-CoA and 2-amino[carboxy-14C]benzoyl-CoA were synthesized enzymatically using 2-aminobenzoyl-CoA synthetase from the same organism. The product was purified by chromatography and characterized by ultraviolet/visible and 1H-NMR spectroscopy. The conversion of 2-aminobenzoyl-CoA catalyzed by the monooxygenase/reductase requires NADH and oxygen, and yields at least two different products depending on the relative concentration of NADH. At [NADH]&lt; Km (40 μM), i.e. [NADH]/[2-aminobenzoyl-CoA] ~ 0.02 0.05, the main product is probably a hydroxylated derivative of 2-aminobenzoyl-CoA, which is characterized by an absorbance maximum around 375 nm. When [NADH]/[2-aminobenzoyl-CoA] ~ 2 5, the predominant product is a non-aromatic coenzyme A thioester (λmax ~ 320 nm). The stoichiometry in this case is 2.1 2.4 mol NADH oxidized (mol oxygen consumed)−1 (mol 2-aminobenzoyl-CoA metabolized)−1. The product is extremely unstable in the acidic pH range and undergoes decarboxylation in a few minutes at pH &lt; 5. Some degree of stabilisation is obtained upon reduction with sodium borohydride, probably resulting in a further reduced non-aromatic coenzyme-A thioester.</dcterms:abstract>
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