Linked Life Data

12393213

Source:http://linkedlifedata.com/resource/pubmed/id/12393213

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2002-10-23
pubmed:abstractText
Zoocin A is a lysostaphin-like streptococcolytic enzyme produced by Streptococcus equi subsp. zooepidemicus 4881 that specifically targets the cell walls of some closely related species. On the basis of sequence homology it was suggested that zoocin A was a domain-structured enzyme with the N-terminal domain responsible for catalysis (CAT) and the C-terminal domain for target recognition (SBD). Polypeptides corresponding to zoocin A (rZooA) and each of the putative domains (rCAT and rSBD) were prepared by use of recombinant technology. The biological activities of each was compared by use of a dye-release assay and a cell-binding assay. Cell wall hydrolysis was shown to be a function of CAT and target recognition a function of the SBD. Expression of the zoocin A immunity factor gene produced cell walls resistant to hydrolysis by either rZooA or its component domains, and with reduced capacity to bind rZooA and rSBD.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0378-1097
pubmed:author
pubmed:issnType
Print
pubmed:day
24
pubmed:volume
215
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
133-8
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2002
pubmed:articleTitle
Functional characterization of domains found within a lytic enzyme produced by Streptococcus equi subsp. zooepidemicus.
pubmed:affiliation
Microbiology Department, University of Otago, P.O. Box 56, 9001, Dunedin, New Zealand. robin.simmonds@stonebow.otago.ac.nz
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't