KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.012 | - |
NADPH | pH 7.5, 15°C | Aspergillus fumigatus | |
0.1 | - |
NADH | pH 7.5, 15°C | Aspergillus fumigatus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Aspergillus fumigatus | Q5SE95 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-ornithine + NADH + H+ + O2 | - |
Aspergillus fumigatus | N5-hydroxy-L-ornithine + NAD+ + H2O | - |
? | |
L-ornithine + NADPH + H+ + O2 | - |
Aspergillus fumigatus | N5-hydroxy-L-ornithine + NADP+ + H2O | - |
? | |
additional information | 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 | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
SidA | - |
Aspergillus fumigatus |
siderophore A | - |
Aspergillus fumigatus |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.6 | - |
NADPH | pH 7.5, 15°C | Aspergillus fumigatus | |
0.73 | - |
NADH | pH 7.5, 15°C | Aspergillus fumigatus |
General Information | Comment | Organism |
---|---|---|
physiological function | enzyme is essential for virulence | Aspergillus fumigatus |
kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
10 | - |
NADH | pH 7.5, 15°C | Aspergillus fumigatus | |
50 | - |
NADPH | pH 7.5, 15°C | Aspergillus fumigatus |