Breakdown of 3-(allylsulfonio)propanoates in bacteria from the Roseobacter group yields garlic oil constituents

• Anuj Kumar Chhalodia and
• Jeroen S. Dickschat

Beilstein J. Org. Chem. 2021, 17, 569–580, doi:10.3762/bjoc.17.51

• acrylic acid (Scheme 3). The obtained DMSP analogues were fed to marine broth agar plate cultures of three strains from the Roseobacter group with fully sequenced genomes, including P. inhibens DSM 17395, Dinoroseobacter shibae DSM 16493, and Oceanibulbus indolifex DSM 14862. In all cases the bacterial

• . Dinoroseobacter shibae additionally encodes genes for the DMSP hydrolase DddD and the DMSP lyase DddL, explaining the formation of 29, while no DMSP hydrolase or lyase is found in O. indolifex. Still, compound 29 is observed within this organism, but in lower quantities than in P. inhibens or D. shibae, and may

• mutational work will be needed for more detailed insights to support our hypotheses regarding the involved enzymes in AllMSP and DAllSP breakdown and will be performed in our laboratories in the future. Experimental Strains and culture condition Phaeobacter inhibens DSM 14862, Dinoroseobacter shibae DSM

Identification of volatiles from six marine Celeribacter strains

• Anuj Kumar Chhalodia,
• Jan Rinkel,
• Dorota Konvalinkova,
• Jörn Petersen and
• Jeroen S. Dickschat

Beilstein J. Org. Chem. 2021, 17, 420–430, doi:10.3762/bjoc.17.38

• and various types of marine algae, e.g., the first described organisms Roseobacter litoralis DSM 6996T and R. denitrificans DSM 7001T were obtained from seaweed [7], while Dinoroseobacter shibae DSM 16493T and Marinovum algicola DSM 10251T are both isolates from the dinoflagellate Prorocentrum lima [8

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

• Lisa Ziesche,
• Jan Rinkel,
• Jeroen S. Dickschat and
• Stefan Schulz

Beilstein J. Org. Chem. 2018, 14, 1309–1316, doi:10.3762/bjoc.14.112

• 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

• , 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. Keywords: Dinoroseobacter shibae

• regulate several physiological traits regulated by cell density, the ‘quorum’ [11][12][13][14][15][16], in roseobacters, e.g., in the production of the antibiotic tropodithietic acid in Phaeobacter inhibens [15] and cell differentiation in Dinoroseobacter shibae [14]. Roseobacter group AHLs are

Isotopically labeled sulfur compounds and synthetic selenium and tellurium analogues to study sulfur metabolism in marine bacteria

• Nelson L. Brock,
• Christian A. Citron,
• Claudia Zell,
• Martine Berger,
• Irene Wagner-Döbler,
• Jörn Petersen,
• Thorsten Brinkhoff,
• Meinhard Simon and
• Jeroen S. Dickschat

Beilstein J. Org. Chem. 2013, 9, 942–950, doi:10.3762/bjoc.9.108

• , Dinoroseobacter shibae DSM 16493T, Labrenzia alexandrii DFL-11T, Roseovarius mucosus DFL-24T, and Hoeflea phototrophica DFL-43T (Supporting Information File 1, Figure S2). The production of methylated selenium volatiles from the selenate and selenite salts was especially pronounced for H. phototrophica from the

• given in Supporting Information File 1, Table S1. Phaeobacter gallaeciensis DSM 17395 [17], Ruegeria pomeroyi DSS-3 (DSM 15171T) [31], Roseobacter denitrificans OCh 114 (DSM 7001T) [32], Oceanibulbus indolifex HEL-45 (DSM 14862T) [33], Dinoroseobacter shibae DFL-12 (DSM 16493T) [34], Labrenzia