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. 1985 Nov 15;232(1):151–160. doi: 10.1042/bj2320151

Purification and properties of uroporphyrinogen III synthase (co-synthetase) from Euglena gracilis.

G J Hart, A R Battersby
PMCID: PMC1152852  PMID: 3936481

Abstract

Uroporphyrinogen III synthase (co-synthetase) purified from Euglena gracilis is a monomer of Mr 38 500 by gel-filtration studies and 31 000 by sodium dodecyl sulphate/polyacrylamide-gel electrophoresis. The pI is apparently in the range 4.8-5.1. No evidence for any cofactors was found, and folate derivatives were shown to be absent; no metal ions appear to be present in the enzyme. The Km for hydroxymethylbilane is in the range 12-40 microM, and the product, uroporphyrinogen III, is an inhibitor. Modification studies suggest that arginine residues are essential for the activity of co-synthetase; lysine residues may also be essential, but histidine, cysteine and tyrosine residues are not.

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Selected References

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