The DOI matches its Crossref record; 10 of the 10 references it cites were found in a registry or an index.
Potent and specific inhibition of glutathione synthesis by buthionine sulfoximine (S-n-butyl homocysteine sulfoximine).
Open accessAbstract
Buthionine sulfoximine (S-n-butyl homocysteine sulfoximine), the most potent of a series of analogs of methionine sulfoximine thus far studied (Griffith, O.W., Anderson, M.E., and Meister, A. (1979) J. Biol. Chem. 254, 1205-1210), inhibited gamma-glutamylcysteine synthetase about 20 times more effectively than did prothionine sulfoximine and at least 100 times more effectively than methionine sulfoximine. The findings support the conclusion that the S-alkyl moiety of the sulfoximine binds at the enzyme site that normally binds the acceptor amino acid. Thus, the affinity of the enzyme for the S-ethyl, S-n-propyl, and S-n-butyl sulfoximines increases in a manner which is parallel to those of the corresponding isosteric acceptor amino acid substrates, i.e. glycine, alanine, and alpha-aminobutyrate. Buthionine sulfoximine did not inhibit glutamine synthetase detectably, nor did it produce convulsions when injected into mice. Injection of buthionine sulfoximine into mice decreased the level of glutathione in the kidney to a greater extent (less than 20% of the control level) than found previously after giving prothionine sulfoximine. alpha-Methyl buthionine sulfoximine was also prepared and found to be almost as effective as buthionine sulfoximine; this compound would not be expected to undergo substantial degradative metabolism. Buthionine sulfoximine and alpha-methyl buthionine sulfoximine may be useful agents for inhibition of glutathione synthesis in various experimental systems.
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In the citing paper
“eprenetapopt may be unique, triggering an increase in turnover of GSH rather than restraining de novo GSH synthesis, as imposed by erastin through its inhibition of cystine uptake or by l-buthionine sulfoximine through inhibition of glutamate-cysteine ligase (40).”
From Eprenetapopt triggers ferroptosis, inhibits NFS1 cysteine desulfurase, and synergizes with serine and glycine dietary restriction (2022) · cites this paper as [40]
In the citing paper
“buthionine sulfoximine (BSO), an inhibitor of glutamate cysteine ligase (GCL), the enzyme required for GSH synthesis, depletes GSH and exhibits anticancer activity”
From The Two Faces of Reactive Oxygen Species in Cancer (2017) · cites this paper as Griffith & Meister 1979
Citations
Cites
Mechanism of inhibition of glutamine synthetase by methionine sulfoximine
Ronzio, R. A., Rowe, W. B., & Meister, A. (1969) · Biochemistry · doi:10.1021/bi00831a038 · Cited by 327
Self-citationGriffith, O. W., Anderson, M. E., & Meister, A. (1979) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)34188-1 · Cited by 172
Self-citationManning, J. M., Moore, S., Rowe, W. B., & Meister, A. (1969) · Biochemistry · doi:10.1021/bi00834a066 · Cited by 166
Self-citationPhosphorylation of methionine sulfoximine by glutamine synthetase.
Ronzio, R. A., & Meister, A. (1968) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.59.1.164 · Cited by 156
Self-citationSekura, R. D., & Meister, A. (1977) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)40500-x · Cited by 149
Self-citationGriffith, O. W., & Meister, A. (1978) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)38077-8 · Cited by 101
Self-citationComputer analysis of the active site of glutamine synthetase
Gass, J. D., & Meister, A. (1970) · Biochemistry · doi:10.1021/bi00808a012 · Cited by 88
Self-citationBentley, H. R., McDermott, E. E., & Whitehead, J. K. (1951) · Proceedings of the Royal Society B Biological Sciences · doi:10.1098/rspb.1951.0021 · Cited by 47
New synthesis of S-alkyl- DL -homocysteines
Kolenbrander, H. M. (1969) · Canadian Journal of Chemistry · doi:10.1139/v69-542 · Cited by 16
Hayahsi, K. (1960) · Chemical and Pharmaceutical Bulletin · doi:10.1248/cpb.8.177 · Cited by 6
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Self-citationGlutathione in plants: an integrated overview
Noctor, G., Mhamdi, A., Chaouch, S., Han, Y., Neukermans, J., Márquez‐García, B., Queval, G., & Foyer, C. H. (2011) · Plant Cell & Environment · doi:10.1111/j.1365-3040.2011.02400.x · Cited by 1,600
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Metabolite profiling identifies a key role for glycine in rapid cancer cell proliferation
Jain, M., Nilsson, R., Sharma, S., Madhusudhan, N., Kitami, T., Souza, A. L., Kafri, R., Kirschner, M. W., Clish, C. B., & Mootha, V. K. (2012) · Science · doi:10.1126/science.1218595 · Cited by 1,403
Metadata
- Authors
- Griffith, O. W., & Meister, A.
- Affiliations
- Cornell University (US)
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1979-08
- Volume
- 254
- Issue
- 16
- Pages
- 7558-7560
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1535828429
- Cited by
- 1,683
- References
- 10
- Citations by year
- 2026: 12 · 2025: 25 · 2024: 33 · 2023: 30 · 2022: 33 · 2021: 34 · 2020: 26 · 2019: 27 · 2018: 28 · 2017: 25 · 2016: 33 · 2015: 35 · 2014: 38 · 2013: 36 · 2012: 29
- FWCI
- 3.97
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Sulfur Compounds in Biology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Glutathione Transferases and Polymorphisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Amino Acid Enzymes and Metabolism
- Keywords
- buthionine sulfoximine, glutathione synthesis inhibition, gamma-glutamylcysteine synthetase, enzyme inhibition, glutathione, glutamine synthetase
- MeSH terms
- Glutamate-Cysteine Ligase, Glutathione, Kinetics, Methionine Sulfoximine, Peptide Synthases, Structure-Activity Relationship
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