Linked Life Data

18671939

Source:http://linkedlifedata.com/resource/pubmed/id/18671939

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2008-8-25
pubmed:abstractText
Gp181 (2237 amino acids) of Pseudomonas aeruginosa bacteriophage phiKZ (Myoviridae) is a structural virion protein, which bears a peptidoglycan hydrolase domain near its C-terminus. This protein is supposed to degrade the peptidoglycan locally during the infection process. Nine deletional mutants allowed delineation of the peptidoglycan hydrolase domain between amino acids 1880-2042 (gp181M8) and analysis of its biochemical properties. Gp181M8 tolerates a high ionic strength (>320mM) and is less sensitive to long thermal treatments compared to the similar phiKZ endolysin. Gp181M8 lysed all tested outer membrane-permeabilized Gram-negative species. The C-terminal distal end (amino acids 2043-2237) enhances the specific activity of gp181M8 threefold, resulting in a twelve times higher activity than commercial hen egg white lysozyme. These biochemical properties suggest that this novel peptidoglycan hydrolase domain may be suitable for enzybiotic applications.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
1090-2104
pubmed:author
pubmed:issnType
Electronic
pubmed:day
3
pubmed:volume
374
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
747-51
pubmed:meshHeading
pubmed:year
2008
pubmed:articleTitle
The structural peptidoglycan hydrolase gp181 of bacteriophage phiKZ.
pubmed:affiliation
Division of Gene Technology, Department of Biosystems, Katholieke Universiteit Leuven, Kasteelpark Arenberg 21, B-3001 Leuven, Belgium.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't