EC Number |
Substrates |
Organism |
Products |
Reversibility |
---|
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 | more |
extending the side chain by one methylene group to L-lysine results in significant NADPH oxidation without formation of the hydroxylated product, indicating that the reaction is uncoupled |
Pseudomonas aeruginosa |
? |
- |
? |
1.14.13.195 | more |
H2O2 formation by NADPH oxidation in the absence of substrate in presence of FAD |
Pseudomonas aeruginosa |
? |
- |
? |
1.14.13.195 | more |
no activity with D-ornithine, N5-formylornithine, L-lysine, L-glutamate, L-glutamine, L-valine, and the tetrapeptide D-Orn-D-Thr-L-Orn-D-Orn, the enzyme performs NADPH oxidation with formation of H2O2, substrate specificity, overview |
Streptomyces coelicolor |
? |
- |
? |
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 |
? |
- |
? |
1.14.13.195 | more |
no activity with D-ornithine, N5-formylornithine, L-lysine, L-glutamate, L-glutamine, L-valine, and the tetrapeptide D-Orn-D-Thr-L-Orn-D-Orn, the enzyme performs NADPH oxidation with formation of H2O2, substrate specificity, overview |
Streptomyces coelicolor A3(2) |
? |
- |
? |
1.14.13.195 | L-lysine + NADPH + H+ + O2 |
- |
Pseudomonas aeruginosa |
L-lysine N6-oxide + NADP+ + H2O |
- |
? |
1.14.13.195 | L-ornithine + NADH + H+ + O2 |
- |
Aspergillus fumigatus |
N5-hydroxy-L-ornithine + NAD+ + H2O |
- |
? |
1.14.13.195 | L-ornithine + NADPH + H+ + O2 |
- |
Pseudomonas fluorescens |
N5-hydroxy-L-ornithine + NADP+ + H2O |
- |
? |