Structural and Functional Validation of Pseudomonas Savastanoi Ethylene Forming Enzymes Reveals Flexibility in 2-Oxoglutarate Binding Mode and Conformation.

Yihong Sun, Siddhant Dhingra, Mark D Allen, Ethan S Z Cheng, Zhihong Zhang, Christopher J Schofield, Lennart Brewitz

Abstract read

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Article in Chembiochem : a European journal of chemical biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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5 · Who and what money

Authors and funding

7 authors.

Yihong SunChemistry Research Laboratory, Department of Chemistry and the Ineos Oxford Institute for Antimicrobial Research, University of Oxford, Oxford, UK.ORCID https://orcid.org/0009-0004-8715-624X

Siddhant DhingraChemistry Research Laboratory, Department of Chemistry and the Ineos Oxford Institute for Antimicrobial Research, University of Oxford, Oxford, UK.ORCID https://orcid.org/0000-0003-2573-2534

Mark D AllenChemistry Research Laboratory, Department of Chemistry and the Ineos Oxford Institute for Antimicrobial Research, University of Oxford, Oxford, UK.

Ethan S Z ChengChemistry Research Laboratory, Department of Chemistry and the Ineos Oxford Institute for Antimicrobial Research, University of Oxford, Oxford, UK.

Zhihong ZhangChemistry Research Laboratory, Department of Chemistry and the Ineos Oxford Institute for Antimicrobial Research, University of Oxford, Oxford, UK.

Christopher J SchofieldChemistry Research Laboratory, Department of Chemistry and the Ineos Oxford Institute for Antimicrobial Research, University of Oxford, Oxford, UK.ORCID https://orcid.org/0000-0002-0290-6565

Lennart BrewitzChemistry Research Laboratory, Department of Chemistry and the Ineos Oxford Institute for Antimicrobial Research, University of Oxford, Oxford, UK.ORCID https://orcid.org/0000-0002-9465-777X

Funding

Biotechnology and Biological Sciences Research Council BB/R000344/1Biotechnology and Biological Sciences Research Council Grant BB/J003018/1Cancer Research UK Grant C8717/A18245Wellcome Trust Grant106244/Z/14/Z

6 · The paper itself

Abstract

Pseudomonas savastanoi pv. phaseolicola PK2 employs an Fe(II)-dependent ethylene/succinate-forming enzyme (PK2 PsEFE) to produce ethylene from 2-oxoglutarate (2OG). Here we report NMR-based assays showing that the putative P. savastanoi pv. glycinea PsEFE, which differs from PK2 PsEFE by a single residue, and the P. savastanoi pv.1449B PsEFE, which differs from PK2 PsEFE by 28 residues and a C-terminal 13-residue truncation, catalyze ethylene production from 2OG. Like the PK2 PsEFE, they catalyze oxidation of naturally occurring 2OG derivatives to give alcohol and diacid products. Crystallographic analysis demonstrates that the overall fold and active site of 1449B PsEFE is similar to that of PK2 PsEFE. Interestingly, 2OG was observed to adopt an atypical inverse metal ion binding mode in complex with 1449B PsEFE:Mn in which its 2-oxoacid group is positioned to interact with the guanidinium group of R277, but not the Mn ion, which substitutes for catalytically active Fe(II). Together with reported crystallographic results, this observation indicates that 2OG metal ion binding modes and conformations at the active sites of 2OG oxygenases can vary, possibly in a functionally or disease relevant manner.

Indexed as

EthylenesKetoglutaric AcidsLyasesPseudomonasBinding SitesCatalytic DomainCrystallography, X-RayModels, MolecularProtein Conformationethyleneethylene forming enzymeEthylenesKetoglutaric AcidsLyases1‐aminocyclopropyl‐1‐carboxylic acid oxidase/ACCO2‐oxoglutarate/2OG/α‐ketoglutarate2‐oxoglutarate/2OG/α‐ketoglutarate dependent dioxygenasebifurcating reaction pathwaysethyleneethylene‐forming enzymeplant developmentYang cycle

Identifiers

PMID41797450

DOI10.1002/cbic.202500702

PMCPMC12968597

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