Hydrolysis of S-2-aminoethylcysteinyl peptide bond by Achromobacter protease I.

Article abstract of DOI:10.1271/bbb.58.215

The substrate specificity of Achromobacter protease I (API) was examined for S-2-aminoethyl(AE)cysteinyl bonds in Bz-AEC-OMe/OEt, Bz-AEC-NH2, and AE-insulin B chain. The protease hydrolyzed all of the tested AE-cysteinyl bonds at the same rate as that of lysyl bonds. Kinetic parameters were estimated for this hydrolysis reaction.

Full text of DOI:10.1271/bbb.58.215

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Hydrolysis of S-2-Aminoethylcysteinyl Peptide Bond
by Achromobacter Protease I
Takeharu Masakia, Toshiyuki Takiyaa, Susumu Tsunasawaab, Shigefumi Kuwaharaa, Fumio
Sakiyamaab & Masami Soejimaa
a Department of Resource Biology, Faculty of Agriculture, Ibaraki University, Ami-machi,
Ibaraki 300–03, Japan
b Institute for Protein Research, Osaka University, Suita, Osaka 565, Japan
Published online: 12 Jun 2014.
To cite this article: Takeharu Masaki, Toshiyuki Takiya, Susumu Tsunasawa, Shigefumi Kuwahara, Fumio Sakiyama &
Masami Soejima (1994) Hydrolysis of S-2-Aminoethylcysteinyl Peptide Bond by Achromobacter Protease I, Bioscience,
Biotechnology, and Biochemistry, 58:1, 215-216, DOI: 10.1271/bbb.58.215
To link to this article: http://dx.doi.org/10.1271/bbb.58.215
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