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Literature summary for 3.4.21.48 extracted from

  • Kominami, E.; Hoffschulte, H.; Leuschel, L.; Maier, K.; Holzer, H.
    The substrate specificity of proteinase B from baker's yeast (1981), Biochim. Biophys. Acta, 661, 136-141.
    View publication on PubMed
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KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.1
-
 benzoyl-Tyr ethyl ester
-
 Saccharomyces cerevisiae
0.8
-
 Acetyl-Tyr ethyl ester
-
 Saccharomyces cerevisiae

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
-
 Saccharomyces cerevisiae
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetyl-Tyr ethyl ester + H2O
-
 Saccharomyces cerevisiae acetyl-Tyr + ethanol
-
 ?
benzoyl-Arg ethyl ester + H2O
-
 Saccharomyces cerevisiae benzoyl-Arg + ethanol
-
 ?
benzoyl-Arg p-nitroanilide + H2O
-
 Saccharomyces cerevisiae benzoyl-Arg + 4-nitroaniline
-
 ?
benzoyl-Ile-Glu-Gly-Arg p-nitroanilide + H2O
-
 Saccharomyces cerevisiae benzoyl-Ile-Glu-Gly-Arg + p-nitroaniline
-
 ?
benzoyl-Tyr ethyl ester + H2O
-
 Saccharomyces cerevisiae benzoyl-Tyr + ethanol
-
 ?
benzoyl-Tyr p-nitroanilide + H2O
-
 Saccharomyces cerevisiae benzoyl-Tyr + 4-nitroaniline
-
 ?
Leu-Trp-Met-Arg-Phe-Ala + H2O preferential attack at Trp-Met Saccharomyces cerevisiae ?
-
 ?
oxidized insulin B chain + H2O initial rapid cleavage step at Leu15-Tyr16 and Phe24-Phe25, slower hydrolysis at Gln4-His5, Leu11-Val12, Tyr16-Leu17, Leu17-Val18 and Arg22-Gly23 and Phe25-Tyr26 Saccharomyces cerevisiae ?
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.1
-
 benzoyl-Tyr ethyl ester
-
 Saccharomyces cerevisiae
9.6
-
 Acetyl-Tyr ethyl ester
-
 Saccharomyces cerevisiae