EC Number   |
|---|
    2.8.1.1 | - |
| 2.8.1.1 | 1.04 A resolution crystal structure displays an exposed active site that is distinct from that of rhodanese and mercaptopyruvate sulfurtransferase |
| 2.8.1.1 | at 2 mM (NH4)2SO4 soluble enzyme has low activity and crystals are stable when substrates are added, at 1.4 mM (NH4)2SO4 crystals rapidly dissolve in 1 mM CN- but are relatively stable in 1 mM S2O32- |
| 2.8.1.1 | composed of two identically folded domains with 13 and 21% identical residues |
| 2.8.1.1 | crystallization in a solution with (NH4)2SO4 at pH 7.3, space group C2 with a: 156.0 A, b: 49.0 A, c: 42.2 A and beta: 98.3° |
| 2.8.1.1 | crystallization in a solution with (NH4)2SO4 at pH 7.9 |
| 2.8.1.1 | homology modeling of structure. The potential active site is located between a central beta strand and an alpha helix. Residues R30, E34 are involved in substrate binding |
| 2.8.1.1 | in the sulfur-free state the catalytic Cys residue adopts two alternate conformations, catalytic mechanism relies primarily on the main-chain conformation of the 230 to 235 active-site loop and on a surrounding strong positive electrostatic field |
| 2.8.1.1 | sitting-drop vapour-diffusion method |
| 2.8.1.1 | solution structure of enzyme detected by NMR spectroscopy. Enzyme contains an additional beta-hairpin not found in other rhodaneses. the enzyme atically active domain belongs to the CDC25 class of phosphatases, sulfide dehydrogenases and stress proteins |
