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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5
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pubmed:dateCreated |
1977-7-29
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pubmed:abstractText |
The results of crosslinking experiments with dimethyl suberimidate and gel filtration binding studies are used to delineate a detailed model for phospholipase A2(phosphatide 2-acyl-hydrolase, EC 3.1.1.4) action in the presence of Ca2+ on mixed micelles of Triton X-100 and phospholipid. Important features of the "dual-phospholipid" model are: (i) the use of the nonionic surfactant as an inert matrix that may influence lipid conformation but does not interact with the enzyme; (ii) the involvement of two lipid molecules in a single cycle of catalysis as an explanation for the "surface dilution" phenomenon; (iii) the requirement of an ordered reaction whereby divalent metal ion binds prior to phospholipid binding; and (iv) the induction by lipid substrate of an asymmetric dimer structure for the enzyme.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/266715-10851,
http://linkedlifedata.com/resource/pubmed/commentcorrection/266715-1194273,
http://linkedlifedata.com/resource/pubmed/commentcorrection/266715-1194274,
http://linkedlifedata.com/resource/pubmed/commentcorrection/266715-13955687,
http://linkedlifedata.com/resource/pubmed/commentcorrection/266715-14964,
http://linkedlifedata.com/resource/pubmed/commentcorrection/266715-234017,
http://linkedlifedata.com/resource/pubmed/commentcorrection/266715-4698263,
http://linkedlifedata.com/resource/pubmed/commentcorrection/266715-4798723,
http://linkedlifedata.com/resource/pubmed/commentcorrection/266715-4857565,
http://linkedlifedata.com/resource/pubmed/commentcorrection/266715-4913206,
http://linkedlifedata.com/resource/pubmed/commentcorrection/266715-5064927,
http://linkedlifedata.com/resource/pubmed/commentcorrection/266715-53,
http://linkedlifedata.com/resource/pubmed/commentcorrection/266715-782347
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0027-8424
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
74
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1950-4
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:266715-Binding Sites,
pubmed-meshheading:266715-Calcium,
pubmed-meshheading:266715-Catalysis,
pubmed-meshheading:266715-Chromatography, Gel,
pubmed-meshheading:266715-Imidazoles,
pubmed-meshheading:266715-Micelles,
pubmed-meshheading:266715-Models, Biological,
pubmed-meshheading:266715-Phospholipases,
pubmed-meshheading:266715-Phospholipids,
pubmed-meshheading:266715-Polyethylene Glycols,
pubmed-meshheading:266715-Snake Venoms,
pubmed-meshheading:266715-Structure-Activity Relationship,
pubmed-meshheading:266715-Time Factors,
pubmed-meshheading:266715-Zinc
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pubmed:year |
1977
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pubmed:articleTitle |
Dual role of interfacial phospholipid in phospholipase A2 catalysis.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.
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