EC Number   |
Subunits |
Reference |
|---|
    2.8.1.12 | ? |
x * 11000, His-tagged subunit MoaD, plus x * 18000, FLAG-tagged subunit MoaE, SDS-PAGE |
-, 760491 |
| 2.8.1.12 | ? |
x * 21600, large sbunit CnxH, SDS-PAGE |
722611 |
| 2.8.1.12 | ? |
x * 29000, FLAG-tagged Moad-MoaE precursor protein, SDS-PAGE |
-, 760491 |
| 2.8.1.12 | ? |
x * 8757.94, recombinant carboxylated MoaD, sequence calculation, x * 8774.03, recombinant thiocarboxylated MoaD, sequence calculation, x * 8757.72, recombinant carboxylated MoaD, mass spectrometry, x * 8774.00, recombinant thiocarboxylated MoaD, mass spectrometry |
722622 |
| 2.8.1.12 | ? |
x * 9600, small subunit CnxG, SDS-PAGE |
722611 |
| 2.8.1.12 | heterotetramer |
2 * 17000 + 2 * 10000, SDS-PAGE |
737944 |
| 2.8.1.12 | heterotetramer |
2 * 6900, MoaD, + 2 * 16500, MoaE, SDS-PAGE, composed of two small MoaD and two large subunits MoaE. Both forms of MoaD, carboxylated and thiocarboxylated, are monomeric and are able to form a heterotetrameric complex after coincubation in equimolar ratios with MoaE, but only the thiocarboxylated MPT synthase complex is able to convert precursor Z in vitro to MPT |
722622 |
| 2.8.1.12 | heterotetramer |
2 * 9700, subunit MOCO1-A, + 2 * 20900, subunit MOCO1-B, SDS-PAGE |
723281 |
| 2.8.1.12 | heterotetramer |
2 * 9800, subunit MOCS2A, + 2 * 20800, subunit MCS2B, SDS-PAGE |
722634 |
| 2.8.1.12 | heterotetramer |
the crystal structure of MPT synthase reveals a heterotetrameric protein in which the C-terminus of each small subunit is inserted into a large subunit to form the active site |
723255 |
