PMID:13129604
| Citation |
Macieira, S, Martins, BM and Huber, R (2003) Oxygen-dependent coproporphyrinogen-III oxidase from Escherichia coli: one-step purification and biochemical characterisation. FEMS Microbiol. Lett. 226:31-7 |
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| 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 37500 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. |
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| Keywords |
Amino Acid Sequence; Coproporphyrinogen Oxidase/chemistry; Coproporphyrinogen Oxidase/genetics; Coproporphyrinogen Oxidase/isolation & purification; Coproporphyrinogen Oxidase/metabolism; Coproporphyrinogens/metabolism; Crystallization; Crystallography, X-Ray; Electrophoresis, Polyacrylamide Gel; Escherichia coli/enzymology; Gene Expression Regulation, Bacterial; Molecular Sequence Data; Protein Subunits/chemistry; Protoporphyrins/metabolism; Recombinant Proteins/genetics; Recombinant Proteins/isolation & purification; Recombinant Proteins/metabolism; Spectrum Analysis |
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