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Crystal Data for a Bacterial Serine Protease

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Abstract

α-LYTIC protease is one of several proteolytic enzymes isolated from culture filtrates of a soil bacillus Sorangium sp. (Myxobacter 405)1. Chemical and kinetic studies of this enzyme have shown many remarkable homologies with the pancreatic serine proteases chymotrypsins A and B, trypsin and elastase. For example, α-lytic protease has exactly the same sequence (.Gly.Asp.Ser*.Gly.Gly.) around the active serine as have the pancreatic enzymes1,2. Moreover, the sequence around the single histidine residue in the enzyme (Val.Thr.Ala.Gly.His.Cys.Gly.)3 closely matches the sequence around His 57 of chymotrypsins A4,5 and B6, and the similar sequences around the corresponding histidine residues of trypsin7,8 and pancreatic elastase9.

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Authors and Affiliations

  1. Department of Biochemistry, University of Alberta, Edmonton, Alberta

    M. N. G. JAMES & L. B. SMILLIE

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  1. M. N. G. JAMES
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  2. L. B. SMILLIE
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JAMES, M., SMILLIE, L. Crystal Data for a Bacterial Serine Protease. Nature 224, 694–695 (1969). https://doi.org/10.1038/224694a0

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