Characterization of the S1 binding site of the glutamic acid-specific protease from Streptomyces griseus.

@article{Stennicke1996CharacterizationOT,
  title={Characterization of the S1 binding site of the glutamic acid-specific protease from Streptomyces griseus.},
  author={Henning R. Stennicke and Jens J. Birktoft and Klaus Breddam},
  journal={Protein science : a publication of the Protein Society},
  year={1996},
  volume={5 11},
  pages={2266-75}
}
The glutamic acid-specific protease from Streptomyces griseus (SGPE) is an 18.4-kDa serine protease with a distinct preference for Glu in the P1 position. Other enzymes characterized by a strong preference for negatively charged residues in the P1 position, e.g., interleukin-1 beta converting enzyme (ICE), use Arg or Lys residues as counterions within the S1 binding site. However, in SGPE, this function is contributed by a His residue (His 213) and two Ser residues (Ser 192 and S216). It is… CONTINUE READING

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Characterization of the gene encoding the glutamic-acid-specific protease of Streptomyces griseus.

Biochemistry and cell biology = Biochimie et biologie cellulaire • 1993
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Leatherbarrow RJ.
3.01. Staines, UK: Erithacus Software Ltd. • 1993

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