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

Autor: Strickland KA; Department of Chemistry, University of Central Florida, Orlando, FL 32816, USA., Martinez Rodriguez B; Department of Chemistry, University of Central Florida, Orlando, FL 32816, USA., Holland AA; Department of Chemistry, University of Central Florida, Orlando, FL 32816, USA., Wagner S; Department of Chemistry, University of Central Florida, Orlando, FL 32816, USA., Luna-Alva M; Department of Chemistry, University of Central Florida, Orlando, FL 32816, USA., Graham DE; Biosciences Division, Oak Ridge National Laboratory, Oak Ridge, TN 37831, USA., Caranto JD; Department of Chemistry, University of Central Florida, Orlando, FL 32816, USA.
Jazyk: angličtina
Zdroj: Beilstein journal of organic chemistry [Beilstein J Org Chem] 2024 Apr 17; Vol. 20, pp. 830-840. Date of Electronic Publication: 2024 Apr 17 (Print Publication: 2024).
DOI: 10.3762/bjoc.20.75
Abstrakt: Linear nitramines (R-N(R')NO 2 ; R' = H or alkyl) are toxic compounds, some with environmental relevance, while others are rare natural product nitramines. One of these natural product nitramines is N -nitroglycine (NNG), which is produced by some Streptomyces strains and exhibits 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 characterized and tested the NNG degradation activity of five Vs NnlA homologs originating from bacteria spanning several classes and isolated from geographically distinct locations. E. coli transformants containing all five homologs converted NNG to nitrite. Four of these five homologs were isolated and characterized. Each isolated homolog exhibited similar oligomerization and heme occupancy as Vs NnlA. Reduction of this heme was shown to be required for NnlA activity in each homolog, and each homolog degraded NNG to glyoxylate, NO 2 - and NH 4 + in accordance with observations of Vs NnlA. It was also shown that NnlA cannot degrade the NNG analog 2-nitroaminoethanol. The combined data strongly suggest that NnlA enzymes specifically degrade NNG and are found in diverse bacteria and environments. These results imply that NNG is also produced in diverse environments and NnlA may act as a detoxification enzyme to protect bacteria from exposure to NNG.
(Copyright © 2024, Strickland et al.)
Databáze: MEDLINE