Linked Life Data

9111933

Source:http://linkedlifedata.com/resource/pubmed/id/9111933

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1997-6-17
pubmed:abstractText
The transphosphatidylation reaction is a unique property of phospholipase D (PLD). In this study, the abilities of plant and mammalian PLDs to utilize straight chain and branched alcohols for transphosphatidylation were analyzed and compared. PLD from peanut utilizes C1 to C8 primary alcohols and gives maximal reaction with butanol. In contrast, PLD from A7r5 vascular smooth muscle cells gives maximal reaction with pentanol and does not utilize octanol. Secondary and tertiary alcohols are not substrates for either enzyme. For branched alcohols, activity increases with distance from the alcohol to the branch point. Competition studies indicated that secondary alcohols cannot access the binding pocket. Thus, PLDs have a water/alcohol binding site with defined steric and hydrophobic parameters.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
1039-9712
pubmed:author
pubmed:issnType
Print
pubmed:volume
41
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
715-24
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
Utilization of alcohols by plant and mammalian phospholipase D.
pubmed:affiliation
Department of Pharmaceutical Sciences, Medical University of South Carolina, Charleston 29425-2303, USA.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S.