Cloned (Comment) | Organism |
---|---|
production of the G298A-beta subunit in Escherichia coli | Azospirillum brasilense |
Protein Variants | Comment | Organism |
---|---|---|
G298A | mutant with an approximately 10fold decrease of the affinity of the enzyme for pyridine nucleotides with little or no effect on the rate of the enzyme reduction by NADPH, maintains the ability to bind NADPH and FAD, is catalytically active in the NADPH:iodonitrotetrazolium oxidoreductase reaction and has a monomeric state, mutation leads to production of insoluble protein under conditions that yield large amounts of soluble wild-type enzyme and to production of smaller amounts of enzyme | Azospirillum brasilense |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
2'-phosphoadenosine-5'-diphospho-5'-beta-D-ribose | inhibitor of the NADPH:iodonitrotetrazolium oxidoreductase reaction of the G298A-beta subunit, competitive with respect to NADPH | Azospirillum brasilense | |
3-Aminopyridine adenine dinucleotide phosphate | inhibitor of the NADPH:iodonitrotetrazolium oxidoreductase reaction of the G298A-beta subunit, competitive with respect to NADPH | Azospirillum brasilense | |
NADP+ | inhibitor of the NADPH:iodonitrotetrazolium oxidoreductase reaction of the G298A-beta subunit, competitive with respect to NADPH | Azospirillum brasilense |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.084 | - |
NADPH | of NADPH: iodonitrotetrazolium oxidoreductase activity of the G298A-beta subunit | Azospirillum brasilense |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Azospirillum brasilense | - |
- |
- |
Purification (Comment) | Organism |
---|---|
of the G298A-beta subunit, using column chromatography on Reactive Red or Amicon Red resins and gel filtration on Ultrogel AcA 34 | Azospirillum brasilense |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-glutamine + 2-oxoglutarate + NADPH + H+ | - |
Azospirillum brasilense | L-glutamate + NADP+ | - |
? |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
flavin | 0.86 mol FAD per mol of mutant beta subunit, 0.83 mol FAD per mol of the wild type species | Azospirillum brasilense | |
NADPH | the C-terminal potential ADP-binding fold of the beta subunit is the NADPH-binding site of the enzyme | Azospirillum brasilense |
Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
---|---|---|---|---|---|
0.0112 | - |
3-Aminopyridine adenine dinucleotide phosphate | inhibitor of the NADPH: iodonitrotetrazolium oxidoreductase reaction of wild type-beta subunit | Azospirillum brasilense | |
0.0227 | - |
2'-phosphoadenosine-5'-diphosphoribose | inhibitor of the NADPH: iodonitrotetrazolium oxidoreductase reaction of wild type-beta subunit | Azospirillum brasilense | |
0.037 | - |
NADP+ | inhibitor of the NADPH: iodonitrotetrazolium oxidoreductase reaction of G298A-beta subunit | Azospirillum brasilense | |
0.128 | - |
3-Aminopyridine adenine dinucleotide phosphate | inhibitor of the NADPH: iodonitrotetrazolium oxidoreductase reaction of G298A-beta subunit | Azospirillum brasilense | |
0.233 | - |
2'-phosphoadenosine-5'-diphosphoribose | inhibitor of the NADPH: iodonitrotetrazolium oxidoreductase reaction of G298A-beta subunit | Azospirillum brasilense |