Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
10
pubmed:dateCreated
2010-11-1
pubmed:abstractText
Lacticin 3147 is a lantibiotic with seven lanthionine bridges across its two component peptides, Ltn? and Ltn?. Although it has been proposed that the eponymous lanthionine and (?-methyl)lanthionine (Lan and meLan) bridges present in lantibiotics make an important contribution to protecting the peptides from thermal or proteolytic degradation, few studies have investigated this link. We have generated a bank of bioengineered derivatives of lacticin 3147, in which selected bridges were removed or converted between Lan and meLan, which were exposed to high temperature or proteolytic enzymes. Although switching Lan and meLan bridges has variable consequences, it was consistently observed that an intact N-terminal lanthionine bridge (Ring A) confers Ltn? with enhanced resistance to thermal and proteolytic degradation.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
1879-1301
pubmed:author
pubmed:copyrightInfo
Copyright © 2010 Elsevier Ltd. All rights reserved.
pubmed:issnType
Electronic
pubmed:day
29
pubmed:volume
17
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1151-60
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
Effect of bioengineering lacticin 3147 lanthionine bridges on specific activity and resistance to heat and proteases.
pubmed:affiliation
Department of Microbiology, University College Cork, Cork, Ireland.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't