Comparison of AaL active site with AiiA, AiiB, and AidC. (A)
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Characterization of a novel N-acylhomoserine lactonase, AidP, from Antarctic Planococcus sp., Microbial Cell Factories
WO2020185861A1 - Proteins and methods for disrupting bacterial communication - Google Patents
Comparison of AaL active site with AiiA, AiiB, and AidC. (A)
Comparison of AaL active site with AiiA, AiiB, and AidC. (A)
Structural and Biochemical Characterization of AaL, a Quorum Quenching Lactonase with Unusual Kinetic Properties
PDF) In silico determination of substrate spectrum of lactonases, hydrolyzing various N-acyl homoserine lactones
Mechanism of the Quorum-Quenching Lactonase (AiiA) from Bacillus thuringiensis. 2. Substrate Modeling and Active Site Mutations
Sequence alignment of the MLLs representatives. Sequence alignment of
Mechanism of the Quorum-Quenching Lactonase (AiiA) from Bacillus thuringiensis. 2. Substrate Modeling and Active Site Mutations
Comparison of amino acid sequences of AidC and five known AiiA-type
Lactonase - an overview
Lactonase - an overview
Frontiers The exceptionally efficient quorum quenching enzyme LrsL suppresses Pseudomonas aeruginosa biofilm production
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