| Autor: |
Widiatningrum, Talitha, Maeda, Sorato, Kataoka, Kunishige, Sakurai, Takeshi |
| Zdroj: |
Biochemistry and Biophysics Reports; September 2015, Vol. 3 Issue: 1 p144-149, 6p |
| Abstrakt: |
A pirin-like protein from a marine denitrifying bacterium, Pseudomonas stutzeriZobell has been heterologously expressed in E. coliand purified to homogeneity with metal-affinity and gel filtration chromatographies. The recombinant pirin-like protein has exhibited quercetinase activities upon the incorporation of a divalent metal ion, while its biological role remains unclear. In the case of Cu2+the holo-protein demonstrated the highest activities and spectroscopic properties typical of type II Cu protein. A 3D-structual model constructed using the crystal structure of human pirin as temperate indicated that the metal biding site is constructed with 3His1Glu located in the consensus sequences in the N-terminal domain. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
|
