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Literature summary for 1.14.13.9 extracted from

  • Oezkilic, Y.; Tuezuen, N.S.
    Mechanism of kynurenine 3-monooxygenase-catalyzed hydroxylation reaction a quantum cluster approach (2019), J. Phys. Chem. A, 123, 3149-3159 .
    View publication on PubMed
Search for more literature for 1.14.13.9

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structure analysis, PDB ID 5NAK Pseudomonas fluorescens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-kynurenine + NADPH + H+ + O2 Pseudomonas fluorescens
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 3-hydroxy-L-kynurenine + NADP+ + H2O
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 ?

Organism

Organism UniProt Comment Textmining
Pseudomonas fluorescens Q84HF5
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Reaction

Reaction Comment Organism Reaction ID
L-kynurenine + NADPH + H+ + O2 = 3-hydroxy-L-kynurenine + NADP+ + H2O mechanism of kynurenine 3-monooxygenase-catalyzed hydroxylation reaction, quantum mechanical calculations on the hydroxylation reaction of the kynurenine pathway, which involves the oxidative half-reaction with low reaction rates, modeling by cluster method, detailed overview. The modeled mechanism involves four successive transformations: Somersault rearrangement (rate-determining step), hydride shift, keto-enol tautomerization, and the dehydration with facile barriers Pseudomonas fluorescens
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-kynurenine + NADPH + H+ + O2
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 Pseudomonas fluorescens 3-hydroxy-L-kynurenine + NADP+ + H2O
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 ?
additional information density functional theory (DFT) calculations in the absence and in the presence of the kynurenine 3-monooxygenase (KMO) enzyme, crystal structure (PDB ID 5NAK)-based calculations involved a quantum cluster model in which the active site of the enzyme with the substrate L-Kyn is represented with 348 atoms. According to the deduced mechanism, KMO-catalyzed hydroxylation reaction takes place with four transformations. In the initial transition state, FAD delivers its peroxy hydroxyl to the L-Kyn ring, creating an sp3-hybridized carbon center. Then, the hydrogen on the hydroxyl moiety is immediately transferred back to the proximal oxygen that remains on FAD. These consequent transformations are in line with the somersault rearrangement previously described for similar enzymatic systems. The second step corresponds to a hydride shift from the sp3-hybridized carbon of the substrate ring to its adjacent carbon, producing the keto form of 3-HK. Then, keto-3-HK is transformed into its enol form (3-HK) with a water-assisted tautomerization. Lastly, FAD is oxidized with a water-assisted dehydration, which also involves 3-HK as a catalyst. Residues Asn54, Pro318, and a crystal water molecule are seen to play significant roles in the proton relays Pseudomonas fluorescens ?
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Subunits

Subunits Comment Organism
homodimer
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 Pseudomonas fluorescens

Synonyms

Synonyms Comment Organism
KMO
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 Pseudomonas fluorescens
pfKMO
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 Pseudomonas fluorescens

Cofactor

Cofactor Comment Organism Structure
FAD
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 Pseudomonas fluorescens
NADPH
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 Pseudomonas fluorescens