Biosynthesis of Branched-Chain Amino Acids in Schizosaccharomyces pombe: Regulation of the Enzymes Involved in Isoleucine, Valine, and Leucine Synthesis

Abstract

The activities and regulation of the enzymes of the synthetic pathway of branched-chain amino acids were investigated in the fission yeast, Schizosaccharomyces pombe. Previous studies had shown the presence of threonine deaminase (TD) and acetohydroxy acid synthetase (AHAS). The remaining isoleucine–valine enzymes, isomeroreductase (IR), dehydrase, and transaminase B, have now been characterized in cell-free extracts, indicating the presence in this yeast of the complete pathway as demonstrated in other microorganisms. α-Isopropylmalate synthetase (IPMS), the first enzyme of the leucine pathway, has properties of a typical regulatory enzyme; it is most active in the pH range 7.5–8.5, but is most sensitive to feedback inhibition by L-leucine at pH 6.5–7.0. Unlike the situation in baker's yeast, only AHAS and IR appeared to be subject to multivalent repression. TD was relatively resistant to any change in level, and AHAS was repressible by valine included in the growth medium. IPMS was repressed when cells were grown in complex medium; leucine alone did not cause repression, and in contrast with baker's yeast, neither did leucine plus threonine or a combination of all three branched-chain amino acids.