Linked Life Data

7042703

Source:http://linkedlifedata.com/resource/pubmed/id/7042703

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1982-7-8
pubmed:abstractText
When microsomal fraction of Saccharomyces cerevisiae was incubated with farnesyl pyrophosphate or presqualene pyrophosphate in the presence of Mn2+, 12,13-cis-dehydrosqualene (DeH2Sq) and some related compounds were found to be formed. Incubation in the presence of NADPH gave rise to only squalene. By heat treatment of the microsomal fraction, the DeH2Sq- and squalene-forming activities were inactivated at approximately the same rate. The elution patterns of both activities upon Sephacryl S-200 chromatography of the enzyme solubilized from the microsomal fraction with taurodeoxycholate coincided completely. These results indicate that DeH2Sq formation in yeast is catalyzed by squalene synthetase. Divalent cation was essential for this reaction and Mn2+ was six times more effective than Mg2+. DeH2Sq formation was also observed when microsomes of pig liver were used instead of yeast microsomal fraction, suggesting that this reaction is a ubiquitous one among the eucaryotes which are capable of synthesizing sterols. Based on these observations, the mechanisms of DeH2Sq and squalene formation are discussed.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0021-924X
pubmed:author
pubmed:issnType
Print
pubmed:volume
91
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
911-21
pubmed:dateRevised
2007-12-19
pubmed:meshHeading
pubmed:year
1982
pubmed:articleTitle
Formation of dehydrosqualene catalyzed by squalene synthetase in Saccharomyces cerevisiae.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't