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Post-translational activation introduces a free radical into pyruvate formate-lyase.
Open accessAbstract
Pyruvate formate-lyase (formate acetyltransferase; EC 2.3.1.54) of Escherichia coli cells is post-translationally interconverted between inactive and active forms. Conversion of the inactive to the active form is catalyzed by an Fe2+-dependent activating enzyme and requires adenosylmethionine and dihydroflavodoxin. This process is shown here to introduce a paramagnetic moiety into the structure of pyruvate formate-lyase. It displays an EPR signal at g = 2 with a doublet splitting of 1.5 mT and could comprise an organic free radical located on an amino acid residue of the polypeptide chain. Hypophosphite was discovered as a specific reagent that destroys both the enzyme radical and the enzyme activity; it becomes covalently bound to the protein. The enzymatic generation of the radical, which is linked to adenosylmethionine cleavage into 5'-deoxyadenosine and methionine, possibly occurs through an Fe-adenosyl complex. These results suggest a radical mechanism for the catalytic cycle of pyruvate formate-lyase.
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Cited by
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Structure and function of the radical enzyme ribonucleotide reductase
Eklund, H., Uhlin, U., Färnegårdh, M., Logan, D. T., & Nordlund, P. (2001) · Progress in Biophysics and Molecular Biology · doi:10.1016/s0079-6107(01)00014-1 · Cited by 323
Metadata
- Authors
- Knappe, J., Neugebauer, F. A., Blaschkowski, H. P., & Gänzler, M.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 1984-03
- Volume
- 81
- Issue
- 5
- Pages
- 1332-1335
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2040907734
- Cited by
- 251
- References
- 0
- FWCI
- 2.93
- Type
- journal article
- Language
- en
- Open access
- green
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- CoChat. (2026). Citation check: Post-translational activation introduces a free radical into pyruvate formate-lyase. https://app.cochat.ai/papers/10.1073/pnas.81.5.1332
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- Knappe, J., Neugebauer, F. A., Blaschkowski, H. P., & Gänzler, M. (1984). Post-translational activation introduces a free radical into pyruvate formate-lyase. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.81.5.1332
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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