EC Number   |
Subunits |
Reference |
|---|
   4.3.2.10 | dimer |
1 * 21653 (subunit HisH) + 1 * 28454 (subunit HisF), calculated from sequence, HisH and HisF proteins form a stable 1:1 dimeric complex that constitutes the IGP synthase holoenzyme |
-, 747052 |
| 4.3.2.10 | dimer |
imidazole glycerol phosphate synthase constitutes a bienzyme complex of the glutaminase subunit HisH and the synthase subunit HisF. Isolated tHisH shows no detectable glutaminase activity but is stimulated by complex formation with tHisF to which either the product imidazole glycerol phosphate or a substrate analogue are bound |
-, 748148 |
| 4.3.2.10 | dimer |
the enzyme is a 1:1 complex of the glutaminase subunit HisH and the cyclase subunit HisF. Subunit HisF contains three distinct internal cavities, which can be identified by xenon-induced chemical shift changes of the neighboring amino acid residues. Two of these cavities are located at the active site at opposite ends of the substrate N'-[(5'-phosphoribulosyl)formimino]-5-aminoimidazole-4-carboxamide ribonucleotide binding groove. The third cavity is located in the interior of the central beta-barrel of HisF and overlaps with the putative ammonia transport channel |
-, 749239 |
| 4.3.2.10 | heterodimer |
the structure of the enzyme provides a model how ammonia is channeled over a distance of about 25 A. The larger part of the putative ammonia tunnel is provided by the interior of the beta barrel of subunit HisF, which has a (betaalpha)8 fold |
-, 749381 |
| 4.3.2.10 | monomer |
1 * 61000, SDS-PAGE |
-, 749228 |
| 4.3.2.10 | monomer |
1 * 61082, calculated from sequence |
-, 749228 |
| 4.3.2.10 | More |
subunit HisH from Zymomonas mobilis (zmHisH) binds with high affinity to the reconstructed subunit HisF from the last universal common ancestor (LUCA-HisF) but not to subunit HisF from Pyrobaculum arsenaticum (paHisF), which differ by 103 residues. Phe74 of LUCA-HisF is decisive for its affinity for zmHisH |
-, 749258 |
