# Biosynthesis of Several Oxyvinylglycine Nonproteinogenic Amino Acids Bearing Unusual Alkoxyamine Bonds

> **NIH NIH F32** · UNIV OF NORTH CAROLINA CHAPEL HILL · 2024 · $73,828

## Abstract

Project Summary
Natural products serve crucial roles in the pharmaceutical industry as drugs or leads for drug compounds.
Generated through secondary metabolism, these molecules impact the virulence, symbiosis, and survival of
microorganisms. The nonproteinogenic oxyvinylglycine amino acids are an interesting class of secondary
metabolites characterized by the presence of a vinyl oxygen moiety. Members of this class, such as 4-(2’-
aminoethoxy)vinylglycine (AVG), are known to arrest germination in plants by inhibiting the pyridoxal 5’-
phosphate (PLP)-dependent enzyme 1-aminocyclopropane-1-carboxylate (ACC) synthase.2 While the
biosynthesis of vinyl ether-bearing oxyvinylglycine nonproteinogenic amino acids including AVG has been
explored, the formation of other members of the family with alternative functional groups remains
undetermined. 4-Formylaminooxyvinylglycine (FVG), an oxyvinylglycine containing an N–O bond, was reported
to have duel herbicidal and bactericidal activity.3,4 The gvg biosynthetic gene cluster in Pseudomonas
fluorescens strain WH6 is responsible for the biosynthesis of FVG and the related compounds
guanidinooxyvinylglycine (GOVG) and aminooxyvinylglycine (AOVG) though the exact biosynthetic mechanism
remains unclear.5,6 In this proposal I will determine the biosynthetic pathways responsible for the formation of
FVG, GOVG, and AOVG. I will use a combination of feeding experiments and in vitro biochemical assays to
determine the substrate and product of each enzyme along the biosynthetic pathway of these three
nonproteinogenic amino acids. The vinyl alkoxyamine is unusual in amino acids, therefore I will characterize
the enzyme responsible for N–O bond construction and determine its chemical mechanism. These studies will
facilitate the bioinformatic discovery of similar oxyvinylglycine nonproteinogenic amino acids. Moreover,
characterization of the iron-dependent enzyme responsible for N–O bond formation will facilitate its use in a
synthetic context to expand the repertoire of oxidative biocatalysts.

## Key facts

- **NIH application ID:** 10906659
- **Project number:** 5F32GM151822-02
- **Recipient organization:** UNIV OF NORTH CAROLINA CHAPEL HILL
- **Principal Investigator:** Joshua Ray Turek-Herman
- **Activity code:** F32 (R01, R21, SBIR, etc.)
- **Funding institute:** NIH
- **Fiscal year:** 2024
- **Award amount:** $73,828
- **Award type:** 5
- **Project period:** 2023-08-01 → 2026-07-31

## Primary source

NIH RePORTER: https://reporter.nih.gov/project-details/10906659

## Citation

> US National Institutes of Health, RePORTER application 10906659, Biosynthesis of Several Oxyvinylglycine Nonproteinogenic Amino Acids Bearing Unusual Alkoxyamine Bonds (5F32GM151822-02). Retrieved via AI Analytics 2026-05-27 from https://api.ai-analytics.org/grant/nih/10906659. Licensed CC0.

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