5780-40-5

Usage

Uses

Used in Organic Synthesis:
(NE)-N-(3-methylbutylidene)hydroxylamine is used as a reactant in the formation of oxime derivatives, which are important in various chemical reactions and processes. Its unique reactivity and structure make it a valuable component in organic synthesis.
Used in Pharmaceutical Research:
NMBHA is being studied for potential applications in the pharmaceutical industry. Its unique chemical properties and reactivity may contribute to the development of new drugs and therapeutic agents.
Used in Agrochemicals:
In addition to its use in organic synthesis and pharmaceuticals, NMBHA is also being explored for potential applications in the agrochemical industry. Its properties may be harnessed to develop new compounds for use in agriculture, such as pesticides or fertilizers.
Used in Chemical Research and Development:
Due to its unique structure and reactivity, (NE)-N-(3-methylbutylidene)hydroxylamine is a valuable tool for chemical research and development. It can be utilized in the creation of new chemical compounds and the study of various chemical reactions and processes.

Upstream product

• 590-86-3 isovaleraldehyde 

Relevant academic research and scientific papers

Synthesis of Isoxazolines and Isoxazoles Inspired by Fipronil

Phenylpyrazoles (or arylpyrazoles) are known to be extremely potent as noncompetitive inhibitors of the GABA-gated chloride channel on the GABA receptor. This project involves the synthesis of novel isoxazole and isoxazoline heterocycles that have similar

Indolyl-3-acetaldoxime dehydratase from the phytopathogenic fungus Sclerotinia sclerotiorum: Purification, characterization, and substrate specificity

The purification and characterization of indolyl-3-acetaldoxime dehydratase produced by the plant fungal pathogen Sclerotinia sclerotiorum is described. The substrate specificity indicates that it is an indolyl-3-acetaldoxime dehydratase (IAD, EC 4.99.1.6), which catalyzes transformation of indolyl-3-acetaldoxime to indolyl-3-acetonitrile. The enzyme showed Michaelis-Menten kinetics and had an apparent molecular mass of 44 kDa. The amino acid sequence of IAD, determined using LC-ESI-MS/MS, identified it as the protein SS1G-01653 from S. sclerotiorum. IADSs was highly homologous (84% amino acid identity) to the hypothetical protein BC1G-14775 from Botryotinia fuckeliana B05.10. In addition, similarity to the phenylacetaldoxime dehydratases from Gibberella zeae (33% amino acid identity) and Bacillus sp. (20% amino acid identity) was noted. The specific activity of IADSs increased about 17-fold upon addition of Na2S2O4 under anaerobic conditions, but in the absence of Na2S2O 4 no significant change was observed, whether aerobic or anaerobic conditions were used. As with other aldoxime dehydratases isolated from microbes, the role of IADSs in fungal plant pathogens is not clear, but given its substrate specificity, it appears unlikely that IADSs is a general xenobiotic detoxifying enzyme.