EC Number   |
Subunits |
Reference |
|---|
    1.2.1.27 | ? |
x * 53700, 2D-PAGE |
656987 |
| 1.2.1.27 | dimer |
2 * 58000, SDS-PAGE |
390219 |
| 1.2.1.27 | dimer |
2 * 69000, gel filtration in presence of SDS |
390219 |
| 1.2.1.27 | homodimer |
2 * 50000 |
-, 722211 |
| 1.2.1.27 | homodimer |
2 * 54000, SDS-PAGE, in solution |
-, 743075 |
| 1.2.1.27 | More |
each subunit consists of three distinct domains: an NAD-binding domain, a catalytic domain, and an oligomerization domain. Identification of key residues important for substrate recognition and tetrahedral intermediate stabilization. Two basic residues (Arg103 and Arg279) and six hydrophobic residues (Phe150, Met153, Val154, Trp157, Met281, and Phe449) are important for tetrahedral intermediate binding. The backbone amide of Cys280 and the side chain amine of Asn149 function as the oxyanion hole during the enzymatic reaction |
-, 743075 |
| 1.2.1.27 | More |
MoMsdh domain architecture, overview |
-, 762976 |
| 1.2.1.27 | tetramer |
4 * 55330, cDNA sequence |
390223 |
| 1.2.1.27 | tetramer |
4 * 58000, SDS-PAGE |
288055 |
| 1.2.1.27 | tetramer |
dimer of dimers, monomer consists of three domains, the dinucleotide binding domain comprising the residues 3123 and 141251, the catalytic domain with residues 252270, and a small domain, with residues 124140 and 471486 |
725485 |
