Linked Life Data

2001385

Source:http://linkedlifedata.com/resource/pubmed/id/2001385

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1991-4-15
pubmed:abstractText
The nearly conserved glycine-30 in porcine pancreatic phospholipase A2 has been replaced by serine. The resulting mutant G30S was expressed in Escherichia coli, purified and characterized. The mutation caused a significant drop in enzymatic activity towards monomeric and aggregated substrates, but had a limited effect on substrate binding. In contrast the affinity for calcium ions, the essential cofactor, was reduced 10-fold. The reduced enzymatic activity is attributed to a reduced stabilization of the transition state. The results are discussed in view of naturally occurring inactive phospholipase A2 homologues from snake venom.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0006-3002
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
1076
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
374-8
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
1991
pubmed:articleTitle
The importance of glycine-30 for enzymatic activity of phospholipase A2.
pubmed:affiliation
Department of Enzymology and Protein Engineering, University of Utrecht, CBLE, University Centre De Uithof, The Netherlands.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't