Abstract
Coproporphyrinogen-III oxidase (CPO) catalyses the conversion of coproporphyrinogen-III to protoporphyrinogen-IX in the haem biosynthetic pathway, and its deficient activity is associated with human hereditary coproporphyria. The 47% sequence identity between the oxygen-dependent CPO from Escherichia coli and its human counterpart makes the bacterial enzyme a good model system for structural studies of this disease. Therefore, we overexpressed and purified to homogeneity the oxygen-dependent CPO from E. coli and its selenomethionine derivative fused with a His 6-tag. Both preparations showed a specific activity of 37 500 U mg −1, had a subunit molecular mass of 35 kDa and behaved as a compact shaped dimer. First crystallisation trials produced plate-shaped diffracting crystals.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
