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Open Access Green as soon as Postprint is submitted to ZB.
The substrate specificity of proteinase B from Baker's yeast.
Biochim. Biophys. Acta 661, 136-141 (1981)
The substrate specificity of proteinase B (EC 3.4.22.9) from Baker's yeast was studied. Experiments with unblocked synthetic peptides indicated that the enzyme has no aminopeptidase activity. The proteinase cleaves trypsin substrates like Bz-Arg-OEt, Bz-Arg-pNA and Bz-Ile-Glu-Gly-Arg-pNA and chymotrypsin substrates like Ac-Tyr-OEt and Bz-Tyr-pNA. The Km value for Ac-Tyr-OEt is similar to that of chymotrypsin A, but the catalytic activity per mol proteinase B amounts to only 1 20 that of chymotrypsin A. Km and kcat for Bz-Arg-OEt are 1 50 and 1 7 as high as the corresponding values determined for trypsin. Proteinase B cleaved the oxidized insulin B chain with an initial rapid cleavage step at Leu(15)-Tyr(16) and Phe(24)-Phe(25). Slower hydrolysis was observed at Gln(4)-His(5), Leu(11)-Val(12) Tyr(16)-Leu(17), Leu(17)-Val(18), Arg(22)-Gly(23) and Phe(25)-Tyr(26). These results suggest that the specificity of proteinase B is comparable to the specificity of porcine chymotrypsin C as well as of trypsin. When the hexapeptide Leu-Trp-Met-Arg-Phe-Ala was used as a substrate for proteinase B, the enzyme preferentially attacked at Arg-Phe and more slowly at Trp-Met.
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Publication type
Article: Journal article
Document type
Scientific Article
Keywords
(baker's Yeast) ; Proteinase B ; Substrate Specificity
ISSN (print) / ISBN
0006-3002
Journal
Biochimica et Biophysica Acta
Quellenangaben
Volume: 661,
Issue: 1,
Pages: 136-141
Publisher
Elsevier
Non-patent literature
Publications
Institute(s)
Institut für Toxikologie und Biochemie