Abstract 1176 Investigating L-DOPA 2,3-Dioxygenase Mechanism in the Pre-Steady State
Lignin is an untapped source of carbon that can be valorized into natural products, feedstocks, and biofuels. Extradiol dioxygenases (EDX) cleave and oxidize the aromatic bond adjacent to the two hydroxyl groups of catecholic monomer units common to lignin, producing desirable synthons. L-DOPA (L-3,4-dihydroxyphenylalanine) 2,3-dioxygenases (DDO) are a small family of EDXs originally isolated from lincomycin biosynthesis. The recently discovered ShjDDO from Streptomyces hygroscopicus jingganensis demonstrates greater kinetic flexibility and catalytic potential compared to previously studied DDOs, which motivated the transient kinetic study of ShjDDO as functions of substrate structure and reaction pH.
Authors
- Keri L. Colabroy (ORCID: https://orcid.org/0000-0002-8045-8403)
- Larryn W. Peterson (ORCID: https://orcid.org/0000-0003-4448-9154)
- Jon Cohen
Publication Details
- Journal
- Journal of Biological Chemistry
- Published
- 2025-05-01
- DOI
- https://doi.org/10.1016/j.jbc.2025.109109
- Primary Topic
- Eicosanoids and Hypertension Pharmacology
- Type
- article
- Field-Weighted Citation Impact
- 0.00