Linked Life Data

3355155

Source:http://linkedlifedata.com/resource/pubmed/id/3355155

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1988-4-27
pubmed:abstractText
Humulene cyclase and caryophyllene cyclase, two enzymes which catalyze the cyclization of farnesyl pyrophosphate to the respective sesquiterpene olefins, have been partially purified from the supernatant fraction of a sage (Salvia officinalis) leaf epidermis extract and separated from each other by a combination of hydrophobic interaction, gel filtration, and ion-exchange chromatography. The molecular weight of both cyclases was estimated by gel filtration to be 57,000 and both cyclases exhibited a pH optimum of 6.5 and preferred Mg2+ (Km approximately 1.5 mM) as the required divalent metal cation. Both enzymes possessed a Km of about 1.7 microM for farnesyl pyrophosphate, were strongly inhibited by p-hydroxymercuribenzoate, and exhibited comparable sensitivities to a variety of other potential inhibitors. The properties of the two sesquiterpene olefin cyclases, which are the first from a higher plant source to be examined in detail, were very similar to each other and to other monoterpene, sesquiterpene, and diterpene cyclases previously described.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0003-9861
pubmed:author
pubmed:issnType
Print
pubmed:volume
261
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
346-56
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1988
pubmed:articleTitle
Partial purification and characterization of two sesquiterpene cyclases from sage (Salvia officinalis) which catalyze the respective conversion of farnesyl pyrophosphate to humulene and caryophyllene.
pubmed:affiliation
Institute of Biological Chemistry, Washington State University, Pullman 99164-6340.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, Non-P.H.S.