EC Number   |
Cofactor |
Reference |
|---|
    2.7.9.3 | 2'(3')-O-(2,4,6-trinitrophenyl)adenosine-5'-triphosphate |
i.e. TNP-ATP, binding analysis of recombinant wild-type and mutant E197D to TNP-ATP, a synthetic fluorescent nucleotide analogue of ATP. The compound is used as a synthetic analogue of the substrate ATP for the monitoring and quantitative analysis of the functional activity of SPS. A non-linear regression analysis of the saturation curve of TNP-ATP binding to D197 SPS fitting to a model with 2 distinct binding sites with KDs different in order. Kinetics, overview |
738466 |
| 2.7.9.3 | alpha,beta-methylene ATP |
i.e. MPCPP, binding structure, overview |
693677 |
| 2.7.9.3 | ATP |
- |
690290, 691179, 691196, 694071, 694096, 694794, 702181, 704580, 705151, 737371, 737653, 737876, 738336, 738466 |
| 2.7.9.3 | ATP |
the ATP-binding site is formed at the subunit interface of the homodimer. Four Asp residues coordinate four metal ions to bind the phosphate groups of AMPCPP. In the free SPS structure, the two loop regions in the ATP-binding site are not ordered, and no enzyme-associated metal is observed. This suggests that ATP binding, metal binding, and the formation of their binding sites are interdependent, Thr221 and Gly222 interact with the gamma-phosphate group of ATP |
693677 |
| 2.7.9.3 | more |
initial characterization of an unknown chromophore. Either the chromophore is directly involved in phosphoryl transfer or indirectly reflects a phosphorylation-dependent conformational change in selenophosphate synthetase |
661912 |
