EC Number   |
Substrates |
Organism |
Products |
Reversibility |
|---|
    1.14.13.195 | L-ornithine + NADPH + H+ + O2 |
one of the initial enzymes in the biosynthetic pathway of pyoverdine I the major siderophore produced by Pseudomonas aeruginosa PAO1 to import iron |
Pseudomonas aeruginosa |
N5-hydroxy-L-ornithine + NADP+ + H2O |
- |
? |
| 1.14.13.195 | L-ornithine + NADPH + H+ + O2 |
PvdA is highly specific for both substrate and coenzyme, PvdA/FAD forms a ternary complex with NADPH and ornithine for catalysis |
Pseudomonas aeruginosa |
N5-hydroxy-L-ornithine + NADP+ + H2O |
- |
? |
| 1.14.13.195 | more |
PvdA is the ornithine hydroxylase, which performs the first enzymatic step in preparation of hydroxamate siderophore derivatives, pyoverdin is the hydroxamate siderophore produced by the opportunistic pathogen Pseudomonas aeruginosa under the iron-limiting conditions of the human host, overview. Poor activity with DL-2,3-diaminopropionic acid and D-ornithine, no activity with L-norleucine, 5-aminopentanoic acid, DL-2,4-diaminobutyric acid, and 1,4-diaminobutane, and no activity with NADH as cofactor, substrate specificity, overview |
Pseudomonas aeruginosa |
? |
- |
? |
| 1.14.13.195 | L-lysine + NADPH + H+ + O2 |
substrate with lower efficiency compared to L-ornithine |
Aspergillus fumigatus |
N6-hydroxy-L-lysine + NADP+ + H2O |
- |
? |
| 1.14.13.195 | L-lysine + NADPH + H+ + O2 |
substrate with lower efficiency compared to L-ornithine |
Aspergillus fumigatus Af293 |
N6-hydroxy-L-lysine + NADP+ + H2O |
- |
? |
| 1.14.13.195 | L-ornithine + NADPH + H+ + O2 |
the enzyme contains the FATGY signature in the putative substrate binding pocket |
Pseudomonas sp. |
N5-hydroxy-L-ornithine + NADP+ + H2O |
- |
? |
| 1.14.13.195 | L-ornithine + NADPH + H+ + O2 |
the enzyme contains the FATGY signature in the putative substrate binding pocket |
Pseudomonas sp. B10 |
N5-hydroxy-L-ornithine + NADP+ + H2O |
- |
? |
| 1.14.13.195 | L-ornithine + NADPH + H+ + O2 |
the enzyme is involved in biosynthesis of N5-acetyl-N5-hydroxy-L-ornithine, a building block of the hydroxamate-type siderophore erythrochelin |
Saccharopolyspora erythraea |
N5-hydroxy-L-ornithine + NADP+ + H2O |
- |
? |
| 1.14.13.195 | more |
the NADPH oxidase activity of the enzyme is tightly coupled to hydroxylamine formation |
Pseudomonas aeruginosa |
? |
- |
? |
| 1.14.13.195 | more |
when the enzyme is reduced with NADPH and reacts with molecular oxygen, a C4a-hydroperoxyflavin intermediate is observed. When the enzyme is reduced with NADH, the intermediate is 2fold less stable. Steady-state kinetic isotope effect values for NADPH and NADH are 3 and 2 , respectively, due to differences in the rate of flavin reduction by these coenzymes. NADP+, and not NAD+, protects the enzyme from proteolysis, suggesting that it induces conformational changes upon binding |
Aspergillus fumigatus |
? |
- |
? |
