Potent and specific inhibition of glutathione synthesis by buthionine sulfoximine (S-n-butyl homocysteine sulfoximine).

Griffith, O.W.; Meister, A.

doi:10.1016/s0021-9258(18)35980-5

Cited by 1,683Sulfur Compounds in BiologyGlutathione Transferases and PolymorphismsAmino Acid Enzymes and Metabolism

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).

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Griffith, O.W., Meister, A.·1979·Journal of Biological Chemistry

DOI 10.1016/s0021-9258(18)35980-5

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Abstract

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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Eprenetapopt may trigger an increase in turnover of GSH rather than restraining de novo GSH synthesis, unlike erastin or l-buthionine sulfoximine.
“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]
Buthionine sulfoximine (BSO), an inhibitor of glutamate cysteine ligase (GCL), depletes GSH and exhibits anticancer activity.
“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

Mechanism of inhibition of glutamine synthetase by methionine sulfoximine
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Inhibition of glutathione biosynthesis by prothionine sulfoximine (S-n-propyl homocysteine sulfoximine), a selective inhibitor of gamma-glutamylcysteine synthetase.
Griffith, O. W., Anderson, M. E., & Meister, A. (1979) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)34188-1 · Cited by 172
Self-citation
Identification of L-methionine S-sulfoximine as the diastereoisomer of L-methionine SR-sulfoximine that inhibits glutamine synthetase
Manning, J. M., Moore, S., Rowe, W. B., & Meister, A. (1969) · Biochemistry · doi:10.1021/bi00834a066 · Cited by 166
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gamma-Glutamylcysteine synthetase. Further purification, "half of the sites" reactivity, subunits, and specificity.
Sekura, R. D., & Meister, A. (1977) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)40500-x · Cited by 149
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“Additionally, buthionine sulfoximine (BSO), an inhibitor of glutamate cysteine ligase (GCL), the enzyme required for GSH synthesis, depletes GSH and exhibits anticancer activity (Andringa et al. 2006, Bailey et al. 1997, Griffith & Meister 1979).”
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[47] Glutathione biosynthesis; γ-glutamylcysteine synthetase from rat kidney
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Mechanism of action, metabolism, and toxicity of buthionine sulfoximine and its higher homologs, potent inhibitors of glutathione synthesis.
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Analytical and preparative separation of the diastereomers of l-buthionine (SR)-sulfoximine, a potent inhibitor of glutathione biosynthesis
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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)
DOI: 10.1016/s0021-9258(18)35980-5
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: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
creativecommons.org/licenses/by/4.0/ (vor, 15044 d)
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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Potent and specific inhibition of glutathione synthesis by buthionine sulfoximine (S-n-butyl homocysteine sulfoximine).

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