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J. Biol. Chem., Vol. 275, Issue 42, 32925-32930, October 20, 2000
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From the The PCD1 nudix hydrolase gene of
Saccharomyces cerevisiae has been cloned and the Pcd1p
protein characterized as a diphosphatase (pyrophosphatase) with
specificity for coenzyme A and CoA derivatives. Oxidized CoA disulfide
is preferred over CoA as a substrate with Km and
kcat values of 24 µM and 5.0 s
The Saccharomyces cerevisiae
PCD1 Gene Encodes a Peroxisomal Nudix Hydrolase Active
toward Coenzyme A and Its Derivatives*
,,¶
Cell Regulation and Signalling Group and
§ Centre for Cell Imaging, School of Biological Sciences,
University of Liverpool, Life Sciences Building,
Liverpool L69 7ZB, United Kingdom
1, respectively, compared with values for
CoA of 280 µM and 4.6 s1
respectively. The products of CoA hydrolysis were 3'-phosphoadenosine 5'-monophosphate and 4'-phosphopantetheine. F ions
inhibited the activity with an IC50 of 22 µM.
The sequence of Pcd1p contains a potential PTS2 peroxisomal targeting
signal. When fused to the N terminus of yeast-enhanced green
fluorescent protein, Pcd1p was shown to locate to peroxisomes by
confocal microscopy. It was also shown to co-localize with peroxisomal thiolase by immunofluorescence microscopy. N-terminal sequence analysis
of the expressed protein revealed the loss of 7 or 8 amino acids,
suggesting processing of the proposed PTS2 signal after import. The
function of Pcd1p may be to remove potentially toxic oxidized CoA
disulfide from peroxisomes in order to maintain the capacity for
-oxidation of fatty acids.
*
This work was supported by Grant F25BJ from the Leverhulme
Trust, by Grant 053038 from the Wellcome Trust, and by grants from Carl
Zeiss Ltd. and the Higher Education Funding Council (to the Centre for
Cell Imaging).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
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