EC Number   |
Metals/Ions |
Reference |
|---|
   1.14.17.3 | Ca2+ |
3.26 mol per mol of bifunctional enzyme |
648703 |
| 1.14.17.3 | copper |
- |
697630, 698481, 699036, 700421 |
| 1.14.17.3 | copper |
a cuproenzyme |
727671, 728178 |
| 1.14.17.3 | copper |
dependent on, copper-deficiency decreases the enzyme activity, tissue copper status, overview |
657678 |
| 1.14.17.3 | copper |
essentially required for activity, 2 atoms bound by 5 conserved His residues and 1 conserved Met residue |
658685 |
| 1.14.17.3 | copper |
inter-copper electron transfer, mechanism, structure, 2 copper atoms per enzyme |
658976 |
| 1.14.17.3 | copper |
metalloenzyme, required for catalysis, bound at the active site |
659847 |
| 1.14.17.3 | copper |
required for activity |
728274 |
| 1.14.17.3 | copper |
the enzyme contains two mononuclear Cu centers |
727016 |
| 1.14.17.3 | copper |
two distinct Cu centers are located in the protein active site. Of the two distinct Cu centers in the protein active site (separated by 11 A), the CuH site, believed to serve primarily as an electron transfer site, is coordinated by three histidines, H107, H108, H172, in a roughly T-shaped geometry. The CuM site, where oxygen binding and hydroxylation occur, has a mixed coordination sphere consisting of two histidines, H242, and H244, and a methionine, M314. Reaction mechanism, overview. Reaction of wild-type enzyme PHM with CO (an oxygen analogue) produces the M-site CO complex, which shows a unique XES spectrum that can be computationally reproduced by including interactions between Cu(I) and the CO ligand. The valence-to-core (VtC) region can serve as a probe of not only ligand speciation, but also offer insight into the coordination geometry, in a fashion similar to XAS pre-edges, and may be sufficiently sensitive to the coordination of exogenous ligands to be useful in the study of reaction mechanisms. Application of X-ray emission spectroscopy to copper proteins via a study of a series of mixed His-Met copper sites where the ligand set varies in a systematic way between the His3 and Met3 limits. The sites are derived from the wild-type peptidylglycine monooxygenase (PHM), two single-site variants which replicate each of its two copper sites (CuM-site and CuH-site), and the transporters CusF and CusB. Structure analysis of copper centers of wild-type and mutant enzymes |
745068 |
