EC Number |
Subunits |
Reference |
---|
1.9.6.1 | ? |
x * 90000 + x * 16000, two-subunit complex, NapA is an 90000 Da catalytic subunit which binds a bis-molybdenum guanosine dinucleoside cofactor and a [4Fe4S] cluster. NapB is an 16000 Da electron-transfer subunit, which in other bacteria binds two c-type haems |
654561 |
1.9.6.1 | ? |
1 * 17000 (NapB) + 1 * 90000 (NapA), the NapA holoenzyme associates with a di-heme c-type cytochrome redox partner (NapB). NapA and NapB proteins purify independently and not as a tight heterodimeric complex. Dissociation constants of 0.015 mM and 0.032 mM are determined for oxidized and reduced NapAB complexes, respectively |
674891 |
1.9.6.1 | ? |
x * 16000 + x * 90000, SDS-PAGE |
684990 |
1.9.6.1 | dimer |
1 * 93000 + 1 * 16000, SDS-PAGE |
697696 |
1.9.6.1 | heterodimer |
1 * 90000 (NapA) + 1 * 16000 (NapB), Nap activity is lost rapidly during the separation of NapA from NapB by anion exchange chromatography, SDS-PAGE |
697968 |
1.9.6.1 | heterodimer |
1 * 17000 + 1 * 87000, SDS-PAGE |
-, 698544 |
1.9.6.1 | heterodimer |
1 * 93309 + 1 * 18924, calculated from sequence |
-, 698544 |
1.9.6.1 | More |
the nap operon of Escherichia coli K-12, encoding a periplasmic nitrate reductase, encodes seven proteins. The catalytic complex in the periplasm, NapANapB receives electrons from the quinol pool via the membrane-bound cytochrome NapC. Like NapA, B and C, NapD, is also essential for Nap activity. None of the remaining three polypeptides, NapF, G and H, which are predicted to encode non-heme, iron-sulfur proteins, are essential for Nap activity |
700256 |
1.9.6.1 | heterodimer |
- |
-, 741958 |
1.9.6.1 | More |
the catalytic subunit of Nap is usually encoded in a nap operon together with accessory proteins involved in its maturation (chaperones) and redox proteins that transfer reducing equivalents from the physiological electron donor (quinone pool) to the active site of the enzyme, nap enzyme domain structure analysis, overview |
-, 742319 |