479050-94-7

Basic information

• Product Name: C16-HSL
• Synonyms: C16:1-DELTA9-(L)-HSL;C16-HSL;N-CIS-HEXADEC-9-ENOYL-L-HOMOSERINE LACTONE;PALMITOLEYL HOMOSERINE LACTONE;N-cis-hexadec-9Z-enoyl-L-Homoserine lactone;(Z)-N-[(3S)-2-oxooxolan-3-yl]hexadec-9-enamide
• CAS NO: 479050-94-7
• Molecular Formula: C20H35NO3
• Molecular Weight: 337.5
• Mol File: 479050-94-7.mol
• Article Data: 1

Chemical Properties

• Appearance: /
• CAS DataBase Reference: C16-HSL(CAS DataBase Reference)
• NIST Chemistry Reference: C16-HSL(479050-94-7)
• EPA Substance Registry System: C16-HSL(479050-94-7)

Safety Data

• Hazardous Substances Data: 479050-94-7(Hazardous Substances Data)

Usage

General Description

C16-HSL, or N-3-Oxooctadecanoyl-homoserine lactone, is a long-chain molecular signal used by many Gram-negative bacteria for intercellular communication, regulation of various genetic traits and virulence. It belongs to the family of N-acyl-homoserine lactones (AHLs), which are involved in quorum sensing, a process by which bacteria sense and respond to changes in their population density. C16-HSL is known to play a role in coordinating complex behaviors such as biofilm formation, motility, and the production of virulence factors. Its structure consists of a long chain fatty acyl tail and a lactone ring, and its synthesis is catalyzed by specific enzymes known as AHL synthases. In various bacterial species, C16-HSL can influence gene expression and coordinate collective behaviors, making it a key signaling molecule in bacterial communication and virulence.

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Relevant articles and documents

Acyl-group specificity of AHL synthases involved in quorum-sensing in Roseobacter group bacteria

N-Acylhomoserine lactones (AHLs) are important bacterial messengers, mediating different bacterial traits by quorum sensing in a cell-density dependent manner. AHLs are also produced by many bacteria of the marine Roseobacter group, which constitutes a large group within the marine microbiome. Often, specific mixtures of AHLs differing in chain length and oxidation status are produced by bacteria, but how the biosynthetic enzymes, LuxI homologs, are selecting the correct acyl precursors is largely unknown. We have analyzed the AHL production in Dinoroseobacter shibae and three Phaeobacter inhibens strains, revealing strain-specific mixtures. Although large differences were present between the species, the fatty acid profiles, the pool for the acyl precursors for AHL biosynthesis, were very similar. To test the acyl-chain selectivity, the three enzymes LuxI1 and LuxI2 from D. shibae DFL-12 as well as PgaI2 from P. inhibens DSM 17395 were heterologously expressed in E. coli and the enzymes isolated for in vitro incubation experiments. The enzymes readily accepted shortened acyl coenzyme A analogs, N-pantothenoylcysteamine thioesters of fatty acids (PCEs). Fifteen PCEs were synthesized, varying in chain length from C4 to C20, the degree of unsaturation and also including unusual acid esters, e.g., 2E,11Z-C18:2-PCE. The latter served as a precursor of the major AHL of D. shibae DFL-12 LuxI1, 2E,11Z-C18:2-homoserine lactone (HSL). Incubation experiments revealed that PgaI2 accepts all substrates except C4 and C20-PCE. Competition experiments demonstrated a preference of this enzyme for C10 and C12 PCEs. In contrast, the LuxI enzymes of D. shibae are more selective. While 2E,11Z-C18:2-PCE is preferentially accepted by LuxI1, all other PCEs were not, except for the shorter, saturated C10-C14-PCEs. The AHL synthase LuxI2 accepted only C14 PCE and 3-hydroxydecanoyl-PCE. In summary, chain-length selectivity in AHLs can vary between different AHL enzymes. Both, a broad substrate acceptance and tuned specificity occur in the investigated enzymes.