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Arch Microbiol. 2007 Mar;187(3):249-56. Epub 2006 Nov 29.

N-acyl homoserine lactones are degraded via an amidolytic activity in Comamonas sp. strain D1.

Author information

1
CNRS, ISV, Bâtiment 23, Avenue de la Terrasse, 91198 Gif-sur-Yvette, France.

Abstract

Comamonas strain D1 enzymatically inactivates quorum-sensing (QS) signal molecules of the N-acyl homoserine lactone (N-AHSL) family, and exhibits the broadest inactivation range of known bacteria. It degrades N-AHSL with acyl-side chains ranging from 4 to 16 carbons, with or without 3-oxo or 3-hydroxy substitutions. N-AHSL degradation yields HSL but not N-acyl homoserine: strain D1 therefore harbors an amidohydrolase activity. Strain D1 is the fifth bacterium species in which an N-AHSL amidohydrolase is described. Consistent with its N-AHSL degradation ability, strain D1 efficiently quenches various QS-dependent functions in other bacteria, such as violacein production by Chromobacterium violaceum and pathogenicity and antibiotic production in Pectobacterium.

PMID:
17136382
DOI:
10.1007/s00203-006-0186-5
[Indexed for MEDLINE]

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