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

BRENDA support

Literature summary 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]

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

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.14.13.195 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
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.14.13.195 Pseudomonas aeruginosa
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
1.14.13.195 flavoprotein
-
 Pseudomonas aeruginosa

Reaction

EC Number Reaction Comment Organism Reaction ID
1.14.13.195 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
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.13.195 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
-
 ?
1.14.13.195 L-ornithine + NADPH + H+ + O2 hydroxylation of the primary amine of ornithine Pseudomonas aeruginosa N5-hydroxy-L-ornithine + NADP+ + H2O
-
 ?
1.14.13.195 additional information H2O2 formation by NADPH oxidation in the absence of substrate in presence of FAD Pseudomonas aeruginosa ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.14.13.195 ornithine hydroxylase
-
 Pseudomonas aeruginosa
1.14.13.195 PvdA
-
 Pseudomonas aeruginosa

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.14.13.195 22 24 assay at Pseudomonas aeruginosa

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.14.13.195 8
-
 assay at Pseudomonas aeruginosa

Cofactor

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

General Information

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