Identification of essential amino acid residues in the nisin dehydratase NisB
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منابع مشابه
Identification of essential amino acid residues in the nisin dehydratase NisB
Nisin is a posttranslationally-modified antimicrobial peptide that has the ability to induce its own biosynthesis. Serines and threonines in the modifiable core peptide part of precursor nisin are dehydrated to dehydroalanines and dehydrobutyrines by the dehydratase NisB, and subsequently cysteines are coupled to the dehydroamino acids by the cyclase NisC. In this study, we applied extensive si...
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The biosynthesis of several classes of ribosomally synthesized and posttranslationally modified peptides involves dehydration of serine and threonine residues. For class I lantibiotics, thiopeptides, and goadsporin, this dehydration is catalyzed by lanthionine biosynthetic enzyme B (LanB) or LanB-like proteins. Although LanB proteins have been studied since 1992, in vitro reconstitution of thei...
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The small antimicrobial peptide nisin, produced by Lactococcus lactis, contains the uncommon amino acid residues dehydroalanine and dehydrobutyrine and five thio ether bridges. Since these structures are posttranslationally formed from Ser, Thr, and Cys residues, it is feasible to study their role in nisin function and biosynthesis by protein engineering. Here we report the development of an ex...
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1 SUBSTRATE RECOGNITION AND SPECIFICITY OF NISB, THE LANTIBIOTIC DEHYDRATASE INVOLVED IN NISIN BIOSYNTHESIS Antonino Mavaro, André Abts, Patrick J. Bakkes, Gert N. Moll, Arnold J. M. Driessen, Sander H.J. Smits and Lutz Schmitt Institute of Biochemistry, Heinrich Heine University Düsseldorf, Universitätsstr. 1, 40225 Düsseldorf, Germany; BiOMaDe Technology Foundation, Nijenborgh 4, 9747 AG Gron...
متن کاملPost-translational modification of therapeutic peptides by NisB, the dehydratase of the lantibiotic nisin.
Post-translationally introduced dehydroamino acids often play an important role in the activity and receptor specificity of biologically active peptides. In addition, a dehydroamino acid can be coupled to a cysteine to yield a cyclized peptide with increased biostability and resistance against proteolytic degradation and/or modified specificity. The lantibiotic nisin is an antimicrobial peptide...
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ژورنال
عنوان ژورنال: Frontiers in Microbiology
سال: 2015
ISSN: 1664-302X
DOI: 10.3389/fmicb.2015.00102