Cloned (Comment) | Organism |
---|---|
recombinant expression of N-terminally His8-MBP-tagged enzyme in Escherichia coli as soluble protein | Amycolatopsis alba |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | steady-state kinetic analysis | Amycolatopsis alba | |
0.107 | - |
L-ornithine | recombinant FAD-reconstituted enzyme-enzyme, pH 7.5, temperature not specified in the publication | Amycolatopsis alba | |
0.305 | - |
L-ornithine | recombinant holo-enzyme, pH 7.5, temperature not specified in the publication | Amycolatopsis alba |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-ornithine + NADH + H+ + O2 | Amycolatopsis alba | - |
N5-hydroxy-L-ornithine + NAD+ + H2O | - |
? | |
L-ornithine + NADPH + H+ + O2 | Amycolatopsis alba | - |
N5-hydroxy-L-ornithine + NADP+ + H2O | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Amycolatopsis alba | - |
- |
- |
Purification (Comment) | Organism |
---|---|
recombinant His-tagged enzyme from Escherichia coli by metal affinity chromatography, depending on the imidazole concentration used, the recombinant enzyme is isolated either in the apo (FAD-free) or holo (FAD-bound) form, cleavage of the tag by TEV protease | Amycolatopsis alba |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
additional information | Amycolatopsis alba cells grown under iron-limiting conditions | Amycolatopsis alba | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-ornithine + NADH + H+ + O2 | - |
Amycolatopsis alba | N5-hydroxy-L-ornithine + NAD+ + H2O | - |
? | |
L-ornithine + NADPH + H+ + O2 | - |
Amycolatopsis alba | N5-hydroxy-L-ornithine + NADP+ + H2O | - |
? | |
additional information | holo (FAD-bound) and apo (FAD-free) forms of the enzyme hydroxylate ornithine. No activity with L-lysine. The enzyme displays very low selectivity for the reduced nicotinamide coenzyme | Amycolatopsis alba | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
abachelin monooxygenase | - |
Amycolatopsis alba |
AMO | - |
Amycolatopsis alba |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.2 | - |
L-ornithine | recombinant FAD-reconstituted enzyme-enzyme, pH 7.5, temperature not specified in the publication | Amycolatopsis alba | |
0.34 | - |
L-ornithine | recombinant holo-enzyme, pH 7.5, temperature not specified in the publication | Amycolatopsis alba |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
assay at | Amycolatopsis alba |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
FAD | - |
Amycolatopsis alba | |
NADH | the enzyme displays very low selectivity for the reduced nicotinamide coenzyme | Amycolatopsis alba | |
NADPH | the enzyme displays very low selectivity for the reduced nicotinamide coenzyme | Amycolatopsis alba |
General Information | Comment | Organism |
---|---|---|
evolution | AMO is a member of the N-hydroxylating monooxygenase (NMO) family of enzymes | Amycolatopsis alba |
metabolism | the enzyme is an N-hydroxylating monooxygenase (NMO) catalyzing the ornithine hydroxylation step in albachelin biosynthesis | Amycolatopsis alba |
kcat/KM Value [1/mMs-1] | kcat/KM Value Maximum [1/mMs-1] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
1.12 | - |
L-ornithine | recombinant holo-enzyme, pH 7.5, temperature not specified in the publication | Amycolatopsis alba | |
1.7 | - |
L-ornithine | recombinant FAD-reconstituted enzyme-enzyme, pH 7.5, temperature not specified in the publication | Amycolatopsis alba |