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The enzymes of bacterial census and censorship

The enzymes of bacterial census and censorship

http://www.wikidata.org/entity/Q27024699

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A Phenylalanine Clamp Controls Substrate Specificity in the Quorum-Quenching Metallo-γ-lactonase from Bacillus thuringiensis Quorum-quenching activity of the AHL-lactonase from Bacillus licheniformis DAHB1 inhibits Vibrio biofilm formation in vitro and reduces shrimp intestinal colonisation and mortality.Isolation of AHL-degrading bacteria from micro-algal cultures and their impact on algal growth and on virulence of Vibrio campbellii to prawn larvae.Structural and Biochemical Characterization of AidC, a Quorum-Quenching Lactonase with Atypical Selectivity Are there acyl-homoserine lactones within mammalian intestines?A high-throughput screen for quorum-sensing inhibitors that target acyl-homoserine lactone synthases Genome sequencing-assisted identification and the first functional validation of N-acyl-homoserine-lactone synthases from the Sphingomonadaceae family.Identification and analysis of the salt tolerant property of AHL lactonase (AiiATSAWB ) of Bacillus species.Acyl-ACP substrate recognition in Burkholderia mallei BmaI1 acyl-homoserine lactone synthase.

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The enzymes of bacterial census and censorship

http://www.wikidata.org/entity/Q27024699

description

2012 nî lūn-bûn

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2012 թուականի Յունուարին հրատարակուած գիտական յօդուած

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2012 թվականի հունվարին հրատարակված գիտական հոդված

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2012年の論文

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2012年論文

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2012年論文

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2012年論文

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2012年論文

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2012年論文

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2012年论文

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name

The enzymes of bacterial census and censorship

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The enzymes of bacterial census and censorship

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The enzymes of bacterial census and censorship

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The enzymes of bacterial census and censorship

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The enzymes of bacterial census and censorship

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The enzymes of bacterial census and censorship

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The enzymes of bacterial census and censorship

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The enzymes of bacterial census and censorship

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The enzymes of bacterial census and censorship

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J.TIBS.2011.10.001

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Trends in Biochemical Sciences

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The enzymes of bacterial census and censorship

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Peter A. Tipton

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Walter Fast

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P2860

Human paraoxonases (PON1, PON2, and PON3) are lactonases with overlapping and distinct substrate specificities

Mechanism of the quorum-quenching lactonase (AiiA) from Bacillus thuringiensis. 2. Substrate modeling and active site mutations

Mechanism of the quorum-quenching lactonase (AiiA) from Bacillus thuringiensis. 1. Product-bound structures

Quinolone signaling in the cell-to-cell communication system of Pseudomonas aeruginosa

Structural identification of a bacterial quorum-sensing signal containing boron

Structural basis and specificity of acyl-homoserine lactone signal production in bacterial quorum sensing

Structure and specificity of a quorum-quenching lactonase (AiiB) from Agrobacterium tumefaciens

The quorum-quenching N-acyl homoserine lactone acylase PvdQ is an Ntn-hydrolase with an unusual substrate-binding pocket

Small-molecule inhibitor binding to an N-acyl-homoserine lactone synthase

Penicillin acylase has a single-amino-acid catalytic centre

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