Advances in Nitrifying Enzymes

doi:10.13560/j.cnki.biotech.bull.1985.2020-0065

Abstract

Abstract:

The nitration of organic compounds especially aromatic nitro-compounds play an important role in chemical production. Aromatic nitro-compounds have become high-value chemical intermediates and industrial products due to their high energy and stable structure. At present,chemical synthesis is the most commonly used nitrification method due to its simple operation,low cost and controllable production conditions. However,this method is of low conversion efficiency and of a lot of waste acid and waste water are produced,and thus causes environmental pollution. These drawbacks restrict the production and application of nitro-compounds. Therefore,it is necessary to seek more efficient and environmental synthesis methods. The application of enzyme catalysis is becoming more and more extensive,and there are abundant microorganisms in nature that can transform nitrogen-containing groups through ammonia or nitrification,providing a repository for enzymatic synthesis of high-energy materials. In this article,we first summarized the types and main functions of nitro-compounds as well as available methods and their deficiencies for synthesizing nitro-compounds. Then we reviewed the types and characteristics of the main nitrifying enzymes in the P450 superfamily,peroxidases and N-oxygenases,analyzed the protein structure and catalytic mechanism of nitrifying enzymes in depth,and listed the directed evolution of nitrifying enzymes. Finally we prospected the research direction of preparing nitro-compounds by using nitrifying enzyme.

Key words: nitration, nitro-compounds, nitrifying enzyme, biosynthesis

ZHAO Lu-yao, CHEN Zhen-ya, HUO Yi-Xin. Advances in Nitrifying Enzymes[J]. Biotechnology Bulletin, 2020, 36(11): 164-172.

Figures/Tables 6

References 61

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蛋白	氧化还原结构	原始产物	突变位点	效果	参考文献
PrnD	2Fe-2S	吡咯尼特林	F312A L277A	底物转化效率提高4.89倍底物转化效率提高3.28倍	[53] [53]
TxtE	血红素	4-硝基色氨酸	融合BM3R和14氨基酸连接肽 R59X H176F/H176Y	增加C5催化位点产量提高3.5倍催化位点由C4转换为C5	[54] [55] [55-56]
AurF	2Fe-2S	p-硝基苯甲酸	T100L L202F	相对活性提高3.14倍相对活性提高3.57倍	[57] [57]

蛋白	氧化还原结构	原始产物	突变位点	效果	参考文献
PrnD	2Fe-2S	吡咯尼特林	F312A L277A	底物转化效率提高4.89倍底物转化效率提高3.28倍	[53] [53]
TxtE	血红素	4-硝基色氨酸	融合BM3R和14氨基酸连接肽 R59X H176F/H176Y	增加C5催化位点产量提高3.5倍催化位点由C4转换为C5	[54] [55] [55-56]
AurF	2Fe-2S	p-硝基苯甲酸	T100L L202F	相对活性提高3.14倍相对活性提高3.57倍	[57] [57]