publication . Article . Other literature type . 2015

Structural and Biochemical Characterization of AidC, a Quorum-Quenching Lactonase with Atypical Selectivity.

Mascarenhas, Romila; Thomas, Pei W.; Wu, Chun-Xiang; Nocek, Boguslaw P.; Hoang, Quyen Q.; Liu, Dali; Fast, Walter;
Open Access
  • Published: 08 Jul 2015 Journal: Biochemistry, volume 54, pages 4,342-4,353 (issn: 0006-2960, eissn: 1520-4995, Copyright policy)
  • Publisher: American Chemical Society (ACS)
Abstract
Quorum-quenching catalysts are of interest for potential application as biochemical tools to interrogate interbacterial communication pathways, as anti-biofouling agents, and as anti-infective agents in plants and animals. Herein, the structure and function of AidC, an N-acyl-L-homoserine (AHL) lactonase from Chryseobacterium, is characterized. Steady-state kinetics show that zinc-supplemented AidC is one of the most efficient wild-type quorum-quenching enzymes characterized to date, with a kcat/KM value of approximately 2 × 106 M−1s−1 for N-heptanoyl-L-homoserine lactone. The enzyme has stricter substrate selectivity and significantly lower KM values (ca. 50 μM...
Subjects
Medical Subject Headings: food and beverages
free text keywords: Biochemistry, Substrate (chemistry), Quorum sensing, Hydrolase, Stereochemistry, Enzyme kinetics, Lactonase, biology.protein, biology, Enzyme, chemistry.chemical_classification, chemistry, Quorum Quenching, Selectivity, Article
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Other literature type . 2015
Biochemistry
Article . 2015
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publication . Article . Other literature type . 2015

Structural and Biochemical Characterization of AidC, a Quorum-Quenching Lactonase with Atypical Selectivity.

Mascarenhas, Romila; Thomas, Pei W.; Wu, Chun-Xiang; Nocek, Boguslaw P.; Hoang, Quyen Q.; Liu, Dali; Fast, Walter;