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Literature summary for 1.14.13.195 extracted from

  • Meneely, K.M.; Barr, E.W.; Bollinger, J.M. Jr.; Lamb, A.L.
    Kinetic mechanism of ornithine hydroxylase (PvdA) from Pseudomonas aeruginosa: substrate triggering of O2 addition but not flavin reduction (2009), Biochemistry, 48, 4371-4376.
    View publication on PubMedView publication on EuropePMC

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information kinetic mechanism of oxidative and reductive half-reactions, stopped-flow kinetics Pseudomonas aeruginosa

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-ornithine + NADPH + H+ + O2 Pseudomonas aeruginosa hydroxylation of the primary amine of ornithine in the initial step of the biosynthesis of siderophore pyoverdin N5-hydroxy-L-ornithine + NADP+ + H2O
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?

Organism

Organism UniProt Comment Textmining
Pseudomonas aeruginosa
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
flavoprotein
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Pseudomonas aeruginosa

Reaction

Reaction Comment Organism Reaction ID
L-ornithine + NADPH + H+ + O2 = N5-hydroxy-L-ornithine + NADP+ + H2O binding of the hydroxylation target is not required to trigger reduction of flavin by NADPH, the reductive half-reaction proceeds in presence and absence of ornithine, reaction of O2 with FADH2 is accelerated 80fold by ornithine, ensuring coupling of NADPH and ornithine, C(4a)-hydroperoxyflavin intermediate, overview Pseudomonas aeruginosa

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-ornithine + NADPH + H+ + O2 hydroxylation of the primary amine of ornithine in the initial step of the biosynthesis of siderophore pyoverdin Pseudomonas aeruginosa N5-hydroxy-L-ornithine + NADP+ + H2O
-
?
L-ornithine + NADPH + H+ + O2 hydroxylation of the primary amine of ornithine Pseudomonas aeruginosa N5-hydroxy-L-ornithine + NADP+ + H2O
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?
additional information H2O2 formation by NADPH oxidation in the absence of substrate in presence of FAD Pseudomonas aeruginosa ?
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?

Synonyms

Synonyms Comment Organism
ornithine hydroxylase
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Pseudomonas aeruginosa
PvdA
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Pseudomonas aeruginosa

Temperature Optimum [┬░C]

Temperature Optimum [┬░C] Temperature Optimum Maximum [┬░C] Comment Organism
22 24 assay at Pseudomonas aeruginosa

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
assay at Pseudomonas aeruginosa

Cofactor

Cofactor Comment Organism Structure
flavin FAD or FMN, required, the reduction of FAD is ornithine-independent Pseudomonas aeruginosa
NADPH H2O2 formation by NADPH oxidation in the absence of substrate in presence of FAD Pseudomonas aeruginosa

General Information

General Information Comment Organism
metabolism the enzyme catalyzes the initial step of the biosynthesis of siderophore pyoverdin Pseudomonas aeruginosa