Pyridoxal Photoenzymes for Organic Synthesis

NIH RePORTER · NIH · R21 · $237,149 · view on reporter.nih.gov ↗

Abstract

7. Project Summary The work described in this proposal aims to advance biocatalytic tools for use in the synthesis of medicinally valuable molecules. We will develop new reaction mechanisms for pyridoxal-dependent enzymes to enable the facile synthesis of non-canonical amino acids through photoexcitation of pyridoxal intermediates involved in the catalysis of threonine aldolase and serine hydroxymethyltransferase. The first goal is to photoexcite the PLP external aldimine enabling it to function as a photoacid. This mechanism will allow these enzymes to use a broader set of 𝛼-, 𝛽-, and 𝛾-amino acids as pronucleophiles. The second goal is to excite the PLP-quinonoid to access a more reducing excited state. This species can reduce alkyl halides, redox-active esters, and cyanoheterocyles to form radicals that can recombine with the PLP-quinonoid radical to produce various non-canonical amino acids. Collectively, these studies will provide a new tool for the synthesis of non- canonical amino acids and serve as the foundation for a new area in photoenzymatic catalysis. The methods and the goals proposed in the Specific Aims can streamline the synthesis of biological probes and drug targets, creating a significant benefit to human health and associated biomedical sciences.

Key facts

NIH application ID
10426622
Project number
1R21GM146043-01
Recipient
CORNELL UNIVERSITY
Principal Investigator
Todd Kurt Hyster
Activity code
R21
Funding institute
NIH
Fiscal year
2022
Award amount
$237,149
Award type
1
Project period
2022-05-01 → 2024-04-30