Regulation of Enzymes Involved in Methionine Biosynthesis in Corynebacterium glutamicum

  • Yeom, Hye-Jin (Graduate School of Biotechnology, Korea University) ;
  • Hwang, Byung-Joon (Graduate School of Biotechnology, Korea University) ;
  • Lee, Myong-Sok (Department of Biological Science, Sookmyung Women's University) ;
  • Kim, Youn-Hee (Department of Oriental Medicine, Semyung University) ;
  • Lee, Heung-Shick (Graduate School of Biotechnology, Korea University, Department of Biotechnology, Korea University)
  • Published : 2004.04.01

Abstract

The regulatory mechanism of methionine biosynthesis in Corynebacterium glutamicum was analyzed at the protein arid gene expression level. O-Acetylhomoserine sulfhydraylase (encoded by metY) was inhibited by 10 mM methionine to a residual activity of 10% level, whereas no such inhibition was found with cystathionine $\gamma$-synthase (encoded by metB) and cystathionine $\beta$-lyase (encoded by metC). The enzymatic activity of homoserine acetyltransferase (encoded by metX) was repressed to a residual activity of 25% level by 10 mM methionine which was added to the growth medium. Cystathionine $\gamma$-synthase and cystathionine $\beta$-lyase were also repressed by 10 mM methionine, but only to a residual activity of 50-70% level. O-Acetylhomoserine sulfhydrylase was very sensitive to repression by 10 mM methionine, showing residual activity of 13%. In addition, homoserine acetyltransferase was also repressed by 10 mM cysteine to 50% of its original activity. No repression of the enzymes by S-adenosyl methionine was observed. The pattern of repression by methionine indicated that the metB and aecD genes might be regulated by a common mechanism, while the metA and metY genes are differently regulated.

Keywords

References

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