Production of dehydroamino acid-containing peptides by Lactococcus lactis. - Wikidata - awgldk - TriplyDB

Production of dehydroamino acid-containing peptides by Lactococcus lactis.

Production of dehydroamino acid-containing peptides by Lactococcus lactis.

http://www.wikidata.org/entity/Q33270794

about

Dissecting structural and functional diversity of the lantibiotic mersacidin Artificial lantipeptides from in vitro translations.Bacterial display and screening of posttranslationally thioether-stabilized peptides.In vitro selection of functional lantipeptides.Ribosomally synthesized and post-translationally modified peptide natural products: overview and recommendations for a universal nomenclature.Site-directed mutations in the lanthipeptide mutacin 1140.Synergistic binding of the leader and core peptides by the lantibiotic synthetase HalM2.Functional Analysis of Genes Involved in the Biosynthesis of Enterocin NKR-5-3B, a Novel Circular Bacteriocin.Post-translational Introduction of D-Alanine into Ribosomally Synthesized Peptides by the Dehydroalanine Reductase NpnJ Didehydrophenylalanine, an abundant modification in the beta subunit of plant polygalacturonases.Use of lantibiotic synthetases for the preparation of bioactive constrained peptides Saturation mutagenesis of TsrA Ala4 unveils a highly mutable residue of thiostrepton A.In vitro reconstitution and substrate specificity of a lantibiotic protease.The importance of the leader sequence for directing lanthionine formation in lacticin 481.Follow the leader: the use of leader peptides to guide natural product biosynthesis.Lacticin 481 synthetase as a general serine/threonine kinase.Investigation of the substrate specificity of lacticin 481 synthetase by using nonproteinogenic amino acids.Distributive and directional behavior of lantibiotic synthetases revealed by high-resolution tandem mass spectrometry.Ribosomally synthesized and post-translationally modified peptide natural products: new insights into the role of leader and core peptides during biosynthesis.Ribosomal peptide natural products: bridging the ribosomal and nonribosomal worlds.The dawning of a 'Golden era' in lantibiotic bioengineering.Increasing the success rate of lantibiotic drug discovery by Synthetic Biology.Advances in the arsenal of tools available enabling the discovery of novel lantibiotics with therapeutic potential.Substrate recognition and specificity of the NisB protein, the lantibiotic dehydratase involved in nisin biosynthesis Easy and rapid purification of highly active nisin.Mechanistic Understanding of Lanthipeptide Biosynthetic Enzymes.Lantibiotic Reductase LtnJ Substrate Selectivity Assessed with a Collection of Nisin Derivatives as Substrates.Chimeric Leader Peptides for the Generation of Non-Natural Hybrid RiPP Products.Biosynthesis and transport of the lantibiotic mutacin 1140 produced by Streptococcus mutans.Influence of shifting positions of Ser, Thr, and Cys residues in prenisin on the efficiency of modification reactions and on the antimicrobial activities of the modified prepeptides.Distinct contributions of the nisin biosynthesis enzymes NisB and NisC and transporter NisT to prenisin production by Lactococcus lactis.Identification of distinct nisin leader peptide regions that determine interactions with the modification enzymes NisB and NisC.Directionality and coordination of dehydration and ring formation during biosynthesis of the lantibiotic nisin.Requirements of the engineered leader peptide of nisin for inducing modification, export, and cleavage.Mechanistic dissection of the enzyme complexes involved in biosynthesis of lacticin 3147 and nisin.Mutagenesis of nisin's leader peptide proline strongly modulates export of precursor nisin.

P2860

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P2860

Production of dehydroamino acid-containing peptides by Lactococcus lactis.

http://www.wikidata.org/entity/Q33270794

description

2007 nî lūn-bûn

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2007 թուականի Յունուարին հրատարակուած գիտական յօդուած

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2007 թվականի հունվարին հրատարակված գիտական հոդված

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2007年の論文

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2007年論文

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2007年論文

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2007年論文

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2007年論文

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2007年論文

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2007年论文

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name

Production of dehydroamino acid-containing peptides by Lactococcus lactis.

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Production of dehydroamino acid-containing peptides by Lactococcus lactis.

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type

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Production of dehydroamino acid-containing peptides by Lactococcus lactis.

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Production of dehydroamino acid-containing peptides by Lactococcus lactis.

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Production of dehydroamino acid-containing peptides by Lactococcus lactis.

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Production of dehydroamino acid-containing peptides by Lactococcus lactis.

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P1433

Applied and Environmental Microbiology

P1476

Production of dehydroamino acid-containing peptides by Lactococcus lactis

@en

P2093

Anneke Kuipers

http://www.w3.org/2001/XMLSchema#string

Gert N Moll

http://www.w3.org/2001/XMLSchema#string

Jenny Wierenga

http://www.w3.org/2001/XMLSchema#string

Oscar P Kuipers

http://www.w3.org/2001/XMLSchema#string

Rick Rink

http://www.w3.org/2001/XMLSchema#string

P2860

Lacticin 481: in vitro reconstitution of lantibiotic synthetase activity.

Post-translational modification of therapeutic peptides by NisB, the dehydratase of the lantibiotic nisin.

Lacticin 481 synthetase phosphorylates its substrate during lantibiotic production.

The mechanism of action of phenylalanine ammonia-lyase: the role of prosthetic dehydroalanine

Three-dimensional structure of membrane and surface proteins.

Biosynthesis and mode of action of lantibiotics.

Structure-activity relationships in the peptide antibiotic nisin: role of dehydroalanine 5.

Improved medium for lactic streptococci and their bacteriophages

The dehydratase activity of lacticin 481 synthetase is highly processive

NisT, the transporter of the lantibiotic nisin, can transport fully modified, dehydrated, and unmodified prenisin and fusions of the leader peptide with non-lantibiotic peptides.

P304

1792-1796

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scholarly article

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10.1128/AEM.02350-06

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P433

6

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P478

73

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P50

Leon D. Kluskens

Arnold J.M Driessen

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2007-01-19T00:00:00Z

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P5875

6541831

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17261515

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P932

1828803

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