Abstract:
:We have explored the mechanism by which an antifungal antibiotic, (S)-2-amino-4-oxo-5-hydroxypentanoic acid, RI-331, preferentially inhibits protein biosynthesis in Saccharomyces cerevisiae, by inhibiting the biosynthesis of the aspartate family of amino acids, methionine, isoleucine and threonine. This inhibition was effected by inhibiting the biosynthesis of their common intermediate precursor homoserine. The target enzyme of RI-331 was homoserine dehydrogenase (EC.1.1.1.3) which is involved in converting aspartate semialdehyde to homoserine in the pathway from aspartate to homoserine. The enzyme is lacking in animals. So the antibiotic is selectively toxic to prototrophic fungi.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Yamaki H,Yamaguchi M,Imamura H,Suzuki H,Nishimura T,Saito H,Yamaguchi Hdoi
10.1016/0006-291x(90)92397-isubject
Has Abstractpub_date
1990-04-30 00:00:00pages
837-43issue
2eissn
0006-291Xissn
1090-2104pii
0006-291X(90)92397-Ijournal_volume
168pub_type
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journal_title:Biochemical and biophysical research communications
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