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An Aspergillus nidulans mutant lacking serine transacetylase: Evidence for two pathways of cysteine biosynthesis

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Summary

cysA− mutants of Aspergillus nidulans lacking serine transacetylase were isolated. cysA− mutants are cysteine auxotrophs only when a second mutation either blocking cystathionine β-synthase (mecA−) or γ-cystathionase (mecB−) is present. These findings prove that homocysteine originating from O-acetylhomoserine and sulfide can be converted not only to methionine, but also to cysteine via the reverse trans-sulfurylation pathway.

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References

  • Arst, H. N., Jr.: Genetic analysis of the first steps of sulphate metabolism in Aspergillus nidulans. Nature (Lond.) 219, 268–270 (1968)

    Article  CAS  Google Scholar 

  • Giovanelli, J., Mudd, S. H.: Transsulfuration in higher plants. Partial purification and properties of γ-cystathionase of spinach. Biochim. biophys. Acta (Amst.) 227, 654–670 (1971)

    Article  CAS  Google Scholar 

  • Kredich, N. M., Tomkins, G. M.: The enzyme synthesis of L-cysteine in E. coli and S. typhimurium. J. biol. Chem. 241, 4955–4965 (1966)

    Article  CAS  Google Scholar 

  • Paszewski, A., Grabski, J.: Studies on β-cystathionase and O-acetylhomoserine sulfhydrylase as the enzymes of alternative methionine biosynthetic pathways in Aspergillus nidulans. Acta biochim. pol. 20, 159–168 (1973)

    CAS  PubMed  Google Scholar 

  • Pieniążek, N. J., Kowalska, I., Stępień, P. P.: Deficiency in methionine adenosyltransferase resulting in limited repressibility of methionine biosynthetic enzymes in Aspergillus nidulans. Molec. gen. Genet. 126, 367–374 (1973)

    Article  Google Scholar 

  • Pieniążek, N. J., Stępień, P. P., Paszewski, A.: An Aspergillus nidulans mutant lacking c cystathionine β-synthase: identity of L-serine sulfhydrylase with cytathionine β-synthase and its distinctness from O-acetyl-L-serine sulfhydrylase. Biochim. biophys. Acta (Amst.) 297, 37–47 (1973)

    Article  Google Scholar 

  • Savin, M. A., Flavin, M., Slaugther, C.: Regulation of homocysteine biosynthesis in Salmonella typhimurium. J. Bact. 111, 547–556 (1972)

    Article  CAS  Google Scholar 

  • Smith, I. K., Thompson, J. F.: Utilisation of S-methylcysteine and methylmercaptan by methionineless mutants of Neurospora and the pathway of their conversion to methionine. II. Enzyme studies. Biochim. biophys. Acta (Amst.) 184, 130–138 (1969)

    Article  CAS  Google Scholar 

  • Wiebers, J. L., Garner, H. R.: Acyl derivatives of homoserine as substrates for homocysteine synthesis in Neurospora crassa, yeast and Escherichia coli. J. Biol. Chem. 42, 5644–5649 (1967)

    Article  Google Scholar 

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Authors and Affiliations

  1. Department of Genetics, Warsaw University, Warszawa, Poland

    Norman J. Pieniążek,  Jerzy Bal,  Ewa Balbin &  Piotr P. Stępień

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  1. Norman J. Pieniążek
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  2. Jerzy Bal
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  3. Ewa Balbin
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  4. Piotr P. Stępień
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Communicated by F. Kaudewitz

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Pieniążek, N.J., Bal, J., Balbin, E. et al. An Aspergillus nidulans mutant lacking serine transacetylase: Evidence for two pathways of cysteine biosynthesis. Molec. Gen. Genet. 132, 363–366 (1974). https://doi.org/10.1007/BF00268575

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  • DOI: https://doi.org/10.1007/BF00268575

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