Linked Life Data

8575454

Source:http://linkedlifedata.com/resource/pubmed/id/8575454

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1996-3-11
pubmed:abstractText
Escherichia coli outer-membrane phospholipase A (OMPLA) is thought to be a member of the class of serine hydrolases, having a classical Asp-His-Ser catalytic triad [Horrevoets, A. J. G., Verheij, H. M. & de Haas, G. H. (1991) Eur. J. Biochem. 198, 247-253]. To identify the histidine residue that is important for catalytic activity, the four histidine residues in E. coli OMPLA that are conserved in other enterobacterial OMPLA enzymes were replaced by cysteine residues using PCR-directed, site-specific mutagenesis. The resulting mutant proteins were all well expressed and displayed heat modifiability, indicating that they were properly folded. Enzyme assays showed that only the His142Cys mutant protein was lacking enzymatic activity. In addition, a His142Gly mutant protein appeared to be inactive. These results show that His142 is important for the enzymatic activity of OMPLA.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0014-2956
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
234
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
934-8
pubmed:dateRevised
2007-7-23
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
A conserved histidine residue of Escherichia coli outer-membrane phospholipase A is important for activity.
pubmed:affiliation
Institute of Biomembranes, Utrecht University, The Netherlands.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't