A pirin-like protein from Pseudomonas stutzeri and its quercetinase activity

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 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.

• Publication year

  2015

• Venue

  Biochemistry and Biophysics Reports

• Publication date

  2015-08-07

• Fields of study

  Biology, Medicine, Chemistry, Environmental Science

• Identifiers
  DOI 10.1016/j.bbrep.2015.08.001PMID 29124178PMCID 5668851
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

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