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Updated: Jul 17, 2025

Utilizing the Ethylene-releasing Compound, 2-Chloroethylphosphonic Acid, as a Tool to Study Ethylene Response in Bacteria
Published on: November 10, 2016
Biological formation of ethylene
Robert P Hausinger1,2, Simahudeen Bathir J S Rifayee3, Midhun G Thomas3
1Department of Microbiology and Molecular Genetics, Michigan State University East Lansing Michigan 48824 USA.
This review details the ethylene-forming enzyme (EFE) in microbes and 1-aminocyclopropane-1-carboxylic acid (ACC) oxidase (ACCO) in plants. Despite distinct functions, both enzymes share structural similarities and require iron for ethylene production.
Area of Science:
- Biochemistry
- Enzymology
- Plant Science
Background:
- Ethylene is a crucial plant hormone involved in various growth and stress responses.
- Two primary biological sources of ethylene are the ethylene-forming enzyme (EFE) in microbes and 1-aminocyclopropane-1-carboxylic acid (ACC) oxidase (ACCO) in plants.
Purpose of the Study:
- To review and compare the structures, biochemical properties, and reaction mechanisms of EFE and ACCO.
- To propose a novel reaction mechanism for ACCO based on mechanistic studies of EFE and known ACCO pathways.
Main Methods:
- Literature review of experimental and computational studies on EFE.
- Analysis of published mechanistic studies on ACCO.
- Comparative analysis of sequence and structural data for EFE and ACCO.
Main Results:
- EFE catalyzes two distinct reactions involving 2-oxoglutarate (2OG) and l-arginine.
- ACCO converts 1-aminocyclopropane-1-carboxylic acid (ACC) to ethylene, a key plant hormone.
- Both EFE and ACCO are structurally related, share sequence homology, and require Fe(II) for activity.
Conclusions:
- Understanding EFE's dual catalytic mechanisms provides insights into related enzymes.
- A novel reaction mechanism for ACCO is proposed, highlighting similarities with EFE.
- This comparative approach enhances our understanding of ethylene biosynthesis across different biological systems.
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