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Chemical Compound Review:

Inhibitor 48 (3S)-4-oxo-3-[[6- (phenylsulfonylaminomethy...

Synonyms: CHEMBL144878, AC1NS24X

Chen, M.X. et al., Bouquin, N. et al., Takashiro, E. et al.

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Disease relevance of Inhibitor 48

A single base change in the acceptor stem of tRNA(3Leu) confers resistance upon Escherichia coli to the calmodulin inhibitor, 48/80 [1].
In this study, inhibitor 48 was the most potent [IC90 (CEM/HIV-1 IIIB) 27 nM] and showed good pharmacokinetics in rats [2].

High impact information on Inhibitor 48

We have isolated several classes of spontaneous mutants resistant to the calmodulin inhibitor 48/80 which inhibits cell division in Escherichia coli K12 [1].
We previously described a mutation feeB1 conferring a temperature-sensitive filamentation phenotype and resistance to the calmodulin inhibitor 48/80 in Escherichia coli, which constitutes a single base change in the acceptor stem of the rare tRNA3Leu recognizing CUA codons [3].

References

A single base change in the acceptor stem of tRNA(3Leu) confers resistance upon Escherichia coli to the calmodulin inhibitor, 48/80. Chen, M.X., Bouquin, N., Norris, V., Casarégola, S., Séror, S.J., Holland, I.B. EMBO J. (1991) [Pubmed]
Structure-activity relationship of HIV-1 protease inhibitors containing alpha-hydroxy-beta-amino acids. Detailed study of P1 site. Takashiro, E., Hayakawa, I., Nitta, T., Kasuya, A., Miyamoto, S., Ozawa, Y., Yagi, R., Yamamoto, I., Shibayama, T., Nakagawa, A., Yabe, Y. Bioorg. Med. Chem. (1999) [Pubmed]
Characterization of an Escherichia coli mutant, feeA, displaying resistance to the calmodulin inhibitor 48/80 and reduced expression of the rare tRNA3Leu. Bouquin, N., Chen, M.X., Kim, S., Vannier, F., Bernard, S., Holland, I.B., Séror, S.J. Mol. Microbiol. (1996) [Pubmed]

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