دورية أكاديمية
Activity assays of NnlA homologs suggest the natural product N-nitroglycine is degraded by diverse bacteria
العنوان: | Activity assays of NnlA homologs suggest the natural product N-nitroglycine is degraded by diverse bacteria |
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المؤلفون: | Kara A. Strickland, Brenda Martinez Rodriguez, Ashley A. Holland, Shelby Wagner, Michelle Luna-Alva, David E. Graham, Jonathan D. Caranto |
المصدر: | Beilstein Journal of Organic Chemistry, Vol 20, Iss 1, Pp 830-840 (2024) |
بيانات النشر: | Beilstein-Institut, 2024. |
سنة النشر: | 2024 |
المجموعة: | LCC:Science LCC:Organic chemistry |
مصطلحات موضوعية: | enzymology, natural products, nitramine, n–n bond, Science, Organic chemistry, QD241-441 |
الوصف: | Linear nitramines (R–N(R′)NO2; 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, NO2− and NH4+ 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. |
نوع الوثيقة: | article |
وصف الملف: | electronic resource |
اللغة: | English |
تدمد: | 1860-5397 |
Relation: | https://doaj.org/toc/1860-5397 |
DOI: | 10.3762/bjoc.20.75 |
URL الوصول: | https://doaj.org/article/330c4cfa06664cb6b0f28e8057e19cf4 |
رقم الأكسشن: | edsdoj.330c4cfa06664cb6b0f28e8057e19cf4 |
قاعدة البيانات: | Directory of Open Access Journals |
تدمد: | 18605397 |
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DOI: | 10.3762/bjoc.20.75 |