Activity assays of NnlA homologs suggest the natural product N-nitroglycine is degraded by diverse bacteria

• Kara A. Strickland,
• Brenda Martinez Rodriguez,
• Ashley A. Holland,
• Shelby Wagner,
• Michelle Luna-Alva,
• David E. Graham and
• Jonathan D. Caranto

Beilstein J. Org. Chem. 2024, 20, 830–840, doi:10.3762/bjoc.20.75

• antibiotic activity towards Gram-negative bacteria. An NNG degrading heme enzyme, called NnlA, has recently been discovered in the genome of Variovorax sp. strain JS1663 (Vs NnlA). Evidence is presented that NnlA and therefore, NNG degradation activity is widespread. To achieve this objective, we

• nitramine. An enzyme, N-nitroglycine lyase A (NnlA), from the bacterium Variovorax sp. strain JS1663 (Vs NnlA) was recently shown to degrade NNG. This strain was enriched from sludge from the Holston Army Ammunition Plant using selective growth media containing NNG as the only carbon and nitrogen source [20

• past 100 years in response to the rise in RDX contamination. Given that Variovorax sp. strain JS1663 was isolated from a nitramine-contaminated sludge, it should be considered if NnlA is promiscuous and can degrade both natural nitramines, such as NNG, and anthropogenic nitramines, such as 2-NAE. We

New variochelins from soil-isolated Variovorax sp. H002

• Jabal Rahmat Haedar,
• Aya Yoshimura and
• Toshiyuki Wakimoto

Beilstein J. Org. Chem. 2024, 20, 692–700, doi:10.3762/bjoc.20.63

• Jabal Rahmat Haedar Aya Yoshimura Toshiyuki Wakimoto Faculty of Pharmaceutical Sciences, Hokkaido University, Kita 12, Nishi 6, Sapporo 060-0812, Japan 10.3762/bjoc.20.63 Abstract The soil bacterial genus Variovorax produce distinct photoreactive siderophores that may play a crucial role in the

• iron cycle within the rhizosphere. This study focused on exploring the natural products of the soil-isolated Variovorax sp. H002, leading to the isolation of variochelins A–E (1–5), a series of lipohexapeptide siderophores. NMR and MS/MS analyses revealed that these siderophores share a common core

• : antimicrobial activity; siderophore; variochelin; Variovorax; Introduction Almost all organisms require iron as a crucial cofactor of enzymes essential for their physiological functions, encompassing primary and secondary metabolisms [1]. However, in an aerobic environment, iron predominantly exists in the

Intermediates and shunt products of massiliachelin biosynthesis in Massilia sp. NR 4-1

• Till Steinmetz,
• Blaise Kimbadi Lombe and
• Markus Nett

Beilstein J. Org. Chem. 2023, 19, 909–917, doi:10.3762/bjoc.19.69

• Burkholderia gladioli, which possesses an unprecedented citrate-derived fatty acid moiety [11]. Furthermore, lipopeptide siderophores with photocleavable moieties, like taiwachelin, were reported from bacteria of the genera Cupriavidus and Variovorax [12][13][14]. The β-proteobacterial genus Massilia was