Linked Life Data

1817255

Source:http://linkedlifedata.com/resource/pubmed/id/1817255

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
8
pubmed:dateCreated
1992-7-6
pubmed:abstractText
We have modified the stability of porcine phospholipase A2 by charge engineering. The mutations are situated at the N-terminal of a major helix and are N89D and N89D/E92Q. This engineering has significantly altered the activity of the enzyme to aggregated and monomeric substrates. A N89D/E92K mutant is more stable but considerably less active than wild type. An N89D mutant is more stable and of similar activity to wild type. The substantial change in activity may be due to direct interaction of residue 92 with aggregated substrate or may be via second calcium binding. Second calcium binding may be more probable as activity against monomers is also affected. Additional calcium binding may therefore be an important way of manipulating the activity of phospholipase A2.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0269-2139
pubmed:author
pubmed:issnType
Print
pubmed:volume
4
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
929-34
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
1991
pubmed:articleTitle
Changes in activity of porcine phospholipase A2 brought about by charge engineering of a major structural element to alter stability.
pubmed:affiliation
Protein Engineering Department, AFRC Institute of Food Research, Shinfield, Reading, UK.
pubmed:publicationType
Journal Article