conserved cysteine residue in yeast uroporphyrinogen decarboxylase in not essential for enzymatic activity

Uroporphyrinogen decarboxylase catalyzes the fifth step of heme biosynthesis in Saccharomyces cerevisiae. Studies utilizing sulfhydryl-specific reagents suggest that the enzyme requires a cysteine residue within the catalytic site. This hypothesis was tested directly by site-directed mutagenesis of...

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Bibliographic Details
Published inCanadian journal of microbiology Vol. 43; no. 8; pp. 792 - 795
Main Authors Di Flumeri, C, Acheson, N.H, Keng, T
Format Journal Article
LanguageEnglish
Published Canada 01.08.1997
Subjects
Alanine - genetics
Cysteine - genetics
Gene Expression Regulation, Enzymologic
Gene Expression Regulation, Fungal
Mutagenesis, Site-Directed
Plasmids
Saccharomyces cerevisiae
Saccharomyces cerevisiae - enzymology
Serine - genetics
Transformation, Genetic
Uroporphyrinogen Decarboxylase - genetics
Uroporphyrinogen Decarboxylase - metabolism
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Summary:Uroporphyrinogen decarboxylase catalyzes the fifth step of heme biosynthesis in Saccharomyces cerevisiae. Studies utilizing sulfhydryl-specific reagents suggest that the enzyme requires a cysteine residue within the catalytic site. This hypothesis was tested directly by site-directed mutagenesis of highly conserved cysteine-52 to serine or alanine. Plasmids containing these mutations were able to complement a hem6 mutant strain. In addition, properties associated with decreased uroporphyrinogen decarboxylase activity were not detected in the mutant strain transformed with these mutant plasmids. These results suggest that the conserved cysteine-52 by itself is not essential for enzymatic activity.
ISSN:0008-4166
1480-3275
DOI:10.1139/m97-114