Type

Journal Article

Authors

Paul D. Cotter
Colin Hill
R Paul Ross
Paula M. O'Connor
Alja Westerbeek
Srinivas Suda

Subjects

Biochemistry

Topics
mass sulfides amino acid substitution alanine matrix assisted laser bacteriocins analogs derivatives beta methyllanthionine lanthionine bioengineering pharmacology anti bacterial agents hot temperature chemistry amino acid sequence lacticin 481 spectrometry peptide hydrolases metabolism

Effect of bioengineering lacticin 3147 lanthionine bridges on specific activity and resistance to heat and proteases. (2010)

Abstract Lacticin 3147 is a lantibiotic with seven lanthionine bridges across its two component peptides, Ltnα and Ltnβ. Although it has been proposed that the eponymous lanthionine and (β-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 Ltnα with enhanced resistance to thermal and proteolytic degradation.
Collections Ireland -> University College Cork -> PubMed

Full list of authors on original publication

Paul D. Cotter, Colin Hill, R Paul Ross, Paula M. O'Connor, Alja Westerbeek, Srinivas Suda

Experts in our system

1
Paul D. Cotter
Teagasc
Total Publications: 253
 
2
Colin Hill
University College Cork
Total Publications: 351
 
3
R Paul Ross
Teagasc
Total Publications: 441
 
4
Paula M. O'Connor
Teagasc
Total Publications: 85