Antifungal activity of Saccharomyces cerevisiae peroxisomal 3-ketoacyl-CoA thiolase
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چکیده
منابع مشابه
Antifungal activity of Saccharomyces cerevisiae peroxisomal 3-ketoacyl-CoA thiolase.
Peroxisomes play an important role in cellular defense systems and generate secondary messengers for cellular communication. Saccharomyces cerevisiae containing oleate-induced peroxisomes were subjected to buffer-soluble extraction and two chromatographic procedures, and a protein with antifungal activity was isolated. The results of MALDI-TOF analysis identified the isolated protein as peroxis...
متن کاملStructural analysis of cDNA for rat peroxisomal 3-ketoacyl-CoA thiolase.
cDNA clones of rat peroxisomal 3-ketoacyl-CoA thiolase were isolated. By blotting analysis using the cDNAs as probes, the mRNA for this enzyme was estimated to be about 1.9-kilobase pairs. Elevation of mRNA levels in the liver with administration of di(2-ethylhexyl)phthalate was also evident. Sequencing analysis revealed 1,272 bases of the open reading frame which encoded 424 amino acid residue...
متن کاملThe 1.8 A crystal structure of the dimeric peroxisomal 3-ketoacyl-CoA thiolase of Saccharomyces cerevisiae: implications for substrate binding and reaction mechanism.
The dimeric, peroxisomal 3-ketoacyl-CoA thiolase catalyses the conversion of 3-ketoacyl-CoA into acyl-CoA, which is shorter by two carbon atoms. This reaction is the last step of the beta-oxidation pathway. The crystal structure of unliganded peroxisomal thiolase of the yeast Saccharomyces cerevisiae has been refined at 1.8 A resolution. An unusual feature of this structure is the presence of t...
متن کاملSaccharomyces cerevisiae peroxisomal thiolase is imported as a dimer.
The active conformation of native peroxisomal 3-ketoacyl-CoA thiolases (EC 2.3.1.16) is homodimeric. We have previously shown that a truncated Saccharomyces cerevisiae thiolase lacking its first 16 N-terminal amino acids fails to be translocated into peroxisomes but assembles into an enzymatically active form in the cytoplasm of a strain with a disrupted nuclear thiolase gene. We now report tha...
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ژورنال
عنوان ژورنال: BMB Reports
سال: 2009
ISSN: 1976-6696
DOI: 10.5483/bmbrep.2009.42.5.281