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Usage

Uses

Used in Pharmaceutical Industry:
4-Pyridinecarboxaldehyde, 3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]-, oxime is used as a pharmaceutical intermediate for the synthesis of various drugs and drug candidates. Its unique structure and functional groups make it a versatile building block in the development of new therapeutic agents.
Used in Chemical Research:
4-Pyridinecarboxaldehyde, 3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]-, oxime is used as a research compound in various chemical studies. Its reactivity and structural features allow scientists to explore its potential applications in the synthesis of new compounds and materials.
Used in Analytical Chemistry:
4-Pyridinecarboxaldehyde, 3-hydroxy-2-methyl-5-[(phosphonooxy)methyl]-, oxime can be used as a derivatizing agent in analytical chemistry. Its ability to form adducts with various analytes makes it a useful tool for enhancing the detection and quantification of target compounds in complex samples.

Upstream product

• 54-47-7 pyridoxal 5'-phosphate 

Relevant academic research and scientific papers

Hydroxamic acids as a novel family of serine racemase inhibitors: Mechanistic analysis reveals different modes of interaction with the pyridoxal-5′-phosphate cofactor

Mammalian serine racemase (SR) is a pyridoxal-5′-phosphate (PLP) dependent enzyme responsible for the biosynthesis of the neurotransmitter D-serine, which activates N-methyl-D-aspartate (NMDA) receptors in the CNS. Aberrant regulation of NMDA receptor signaling has been implicated in a variety of neuropathologies, and inhibitors of SR would therefore be a worthwhile tool for further investigation or treatment of such conditions. Here, we identify a series of small aliphatic hydroxamic acids (HAs) that act as potent SR inhibitors. However, specificity studies showed that some of these HAs can act as nonspecific inhibitors of PLP-dependent enzymes. We employed NMR, MS, and UV/vis spectroscopic techniques to reveal that the nonspecific effect is likely due to irreversible interaction of the HA moiety with PLP to form aldoxime species. We also characterize L-aspartic acid β-hydroxamate as a competitive and selective SR inhibitor that could be used as a scaffold for further inhibitor development. 2009 American Chemical Society.