Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
12
pubmed:dateCreated
1990-10-9
pubmed:abstractText
Candida tropicalis peroxisomes contain a 905-residue trifunctional enzyme with hydratase-dehydrogenase-epimerase activity that is important in fatty acid beta-oxidation. At its amino terminus are two tandem copies of an approximately 280 residue domain of unknown function. We provide evidence that this domain is homologous to oxidoreductases used for metabolizing sugars and synthesizing antibiotics and steroids such as estradiol, androstenedione, corticosterone, and hydrocortisone. The trifunctional enzyme shows no sequence similarity to the bifunctional hydratase-dehydrogenase found in animal peroxisomes and plant glyoxysomes, which are homologs of each other. We suggest that the C. tropicalis trifunctional enzyme and the animal and plant bifunctional enzymes have different ancestors.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0892-6638
pubmed:author
pubmed:issnType
Print
pubmed:volume
4
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
3028-32
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1990
pubmed:articleTitle
A common ancestor for Candida tropicalis and dehydrogenases that synthesize antibiotics and steroids.
pubmed:affiliation
Department of Medicine, University of California, San Diego, La Jolla 92093-0623.
pubmed:publicationType
Journal Article