Letter | Published:

Amino-acid Sequence about the Reactive Serine of a Proteolytic Enzyme from Bacillus subtilis

Naturevolume 187pages872873 (1960) | Download Citation

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Abstract

AN increasing number of hydrolytic enzymes have been reported to be inhibited by diisopropylphosphorofluoridate. Where the resulting diisopropylphosphoenzyme has been investigated, the phosphate was isolated in the form of phospho-serine peptides and the amino-acid sequence about the reactive serine has been determined in several cases. Trypsin1 chymotrypsin2–4, elastase5,6 and thrombin7 have the sequence Gly.Asp.Ser.Gly., while horse liver aliesterase8 and pseudocholinesterase9 have Gly.Glu.Ser.-Ala.Gly. The proteolytic enzyme subtilisin was isolated from a strain of B. subtilis by Güntelberg and Ottesen10 and they recorded its inhibition by diisopropylphosphorofluoridate, while Matsubara11 obtained a phospho-peptide from strain N1 but did not report any sequence. The present communication deals with an investigation of the enzyme from Novo Terapeutisk Laboratorium known as ‘bacterial trypsin’, which is similar to, but distinguishable from, the original subtilisin.

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References

  1. 1

    Dixon, G. H., Kauffman, D. L., and Neurath, H., J. Amer. Chem. Soc., 80, 1260 (1958).

  2. 2

    Turba, F., and Gundlach, G., Biochim. Z., 327, 186 (1955).

  3. 3

    Schaffer, N. K., Simet, L., Harshman, S., Engle, R. R., and Drisko, R. W., J. Biol. Chem., 225, 197 (1957).

  4. 4

    Oosterbaan, R. A., Kunst, P., Van Rotterdam, J., and Cohen, J. A., Biochim. Biophys. Acta, 27, 549 (1958).

  5. 5

    Hartley, B. S., Naughton, M. A., and Sanger, F., Biochim. Biophys. Acta, 34, 243 (1959).

  6. 6

    Naughton, M. A., Sanger, F., Hartley, B. S., and Shaw, D. C., Biochem. J., 77, 149 (1960).

  7. 7

    Gladner, J. A., and Laki, K., J. Amer. Chem. Soc., 80, 1264 (1958).

  8. 8

    Jansz, H. S., Posthumus, C. H., and Cohen, J. A., Biochim. Biophys. Acta, 33, 396 (1959).

  9. 9

    Jansz, H. S., Brons, D., and Warringa, M. G. P. J., Biochim. Biophys. Acta, 34, 573 (1959).

  10. 10

    Güntelbarg, A. V., and Ottesen, M., C.R. Lab. Carlsberg, Ser. Chim., 29, 36 (1953).

  11. 11

    Matsubara, H., J. Biochem. (Japan), 46, 107 (1959).

  12. 12

    Harris, J. I., and Roos, P., Biochem. J., 71, 434 (1959).

  13. 13

    Nicolet, B. H., and Shinn, L. A., J. Amer. Chem. Soc., 61, 161 (1939).

  14. 14

    Discussed in Symposium on Enzyme Reaction Mechanisms, J. Cell. and Comp. Physiol., 54, Supp. 1 (1959).

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Author notes

  1. F. SANGER: Member of the external staff of the Medical Research Council.

  2. D. C. SHAW: Hackett Student from the University of Western Australia and on leave from C.S.I.R.O. Wool Research Laboratories, Australia.

Affiliations

  1. Department of Biochemistry, University of Cambridge

    • F. SANGER
    •  & D. C. SHAW

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https://doi.org/10.1038/187872a0

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