Regulation of enzymes involved in methionine biosynthesis in Corynebacterium glutamicum
- Authors
- Yeom, HJ; Hwang, BJ; Lee, MS; Kim, Y; Lee, HS
- Issue Date
- Apr-2004
- Publisher
- KOREAN SOC MICROBIOLOGY & BIOTECHNOLOGY
- Keywords
- Corynebacterium glutamicum; methionine; homoserine acetyltransferase; cystathionine gamma-synthase; cystathionine beta-lyase
- Citation
- JOURNAL OF MICROBIOLOGY AND BIOTECHNOLOGY, v.14, no.2, pp 373 - 378
- Pages
- 6
- Journal Title
- JOURNAL OF MICROBIOLOGY AND BIOTECHNOLOGY
- Volume
- 14
- Number
- 2
- Start Page
- 373
- End Page
- 378
- URI
- https://scholarworks.sookmyung.ac.kr/handle/2020.sw.sookmyung/15892
- ISSN
- 1017-7825
1738-8872
- Abstract
- The regulatory mechanism of methionine biosynthesis in Corynebacterium glutamicum was analyzed at the protein and 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 cystathioninebeta-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.
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