PMID: 2492941Feb 1, 1989Paper

Studies on uroporphyrinogen decarboxylase of etiolated Euglena gracilis Z

European Journal of Biochemistry
A A JuknatH Ippen

Abstract

1. A 423-fold purified fraction of uroporphyrinogen decarboxylase (EC 4.1.1.37) showing a specific activity of 770 units/mg protein has been employed in order to study some properties in etiolated Euglena gracilis Z. 2. Uroporphyrinogen decarboxylase has a relative molecular mass of 54,000, an optimum pH of 7.2 and exhibits Michaelis-Menten kinetics, employing both uroporphyrinogen I and uroporphyrinogen III as substrates. 3. Anaerobic conditions seem not to be necessary for uroporphyrinogen decarboxylase activity. Neither EDTA nor cysteine affected enzyme activity, whereas dithiothreitol produced a remarkable activation of coproporphyrinogen formation. 4. Kinetic data employing both substrates showed an accumulation of porphyrinogen (i.e. hexa- and hepta-porphyrin) containing six or seven COOH groups, depending on the uroporphyrinogen concentration used. 5. An unusual elution profile of the intermediates on Sephacryl S-200 was found.

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Citations

May 15, 2007·Canadian Journal of Microbiology·Angela B JuárezMaría Del C Ríos de Molina
Jun 1, 1997·Protein Science : a Publication of the Protein Society·J D PhillipsC P Hill
Jan 1, 1992·DNA Sequence : the Journal of DNA Sequencing and Mapping·J A KielG Venema

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