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Literature summary for 1.14.13.39 extracted from
- Kinetic unfolding mechanism of the inducible nitric oxide synthase oxygenase domain determined by time-resolved electrospray mass spectrometry (2005), Biochemistry, 44, 2276-2283.
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Iron | heme iron | Mus musculus |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Mus musculus | - |
- |
- |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| dimer | subunit disassembly and unfolding of the protein following a pH jump from 7.5 to 2.8 | Mus musculus |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| inducible nitric oxide synthase | - |
Mus musculus |
| iNOS | - |
Mus musculus |
pH Stability
| pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|
| additional information | - |
subunit disassembly and unfolding of the protein following a pH jump from 7.5 to 2.8, kinetic unfolding mechanism of the inducible enzymes' oxygenase domain, the initial step of the reaction is the disruption of the iNOSCOD dimer, to generate heme-bound monomeric species in various degrees of unfolding, which is accompanied by the loss of two tetrahydrobiopterin cofactors, subsequent heme loss generates monomeric apoproteins exhibiting various degrees of unfolding, modeling of the denaturation process, overview | Mus musculus |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| NADPH | - |
Mus musculus | |
| tetrahydrobiopterin | - |
Mus musculus | |
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