A pirin-like protein from Pseudomonas stutzeri and its quercetinase activity.
| Autor: | Widiatningrum T; Graduate School of Natural Science and Technology, Kanazawa University, Kakuma, Kanazawa 920-1192, Japan., Maeda S; Graduate School of Natural Science and Technology, Kanazawa University, Kakuma, Kanazawa 920-1192, Japan., Kataoka K; Graduate School of Natural Science and Technology, Kanazawa University, Kakuma, Kanazawa 920-1192, Japan., Sakurai T; Graduate School of Natural Science and Technology, Kanazawa University, Kakuma, Kanazawa 920-1192, Japan. |
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| Jazyk: | angličtina |
| Zdroj: | Biochemistry and biophysics reports [Biochem Biophys Rep] 2015 Aug 07; Vol. 3, pp. 144-149. Date of Electronic Publication: 2015 Aug 07 (Print Publication: 2015). |
| DOI: | 10.1016/j.bbrep.2015.08.001 |
| Abstrakt: | A pirin-like protein from a marine denitrifying bacterium, Pseudomonas stutzeri Zobell has been heterologously expressed in E. coli and 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 Cu 2+ 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: | MEDLINE |
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