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Literature summary for 3.4.24.27 extracted from

  • Nakanishi, K.; Kimura, Y.; Matsuno, R.
    Kinetics and equilibrium of enzymatic synthesis of peptides in aqueous/organic biphasic systems. Thermolysin-catalyzed synthesis of N-(benzyloxycarbonyl)-L-aspartyl-L-phenylalanine methyl ester [published erratum appears in Eur J Biochem 1987 Sep 15;167(3):601] (1986), Eur. J. Biochem., 161, 541-549.
    View publication on PubMed
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Inhibitors

Inhibitors Comment Organism Structure
dipeptides overview, temperature dependence, pH-dependence Bacillus thermoproteolyticus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.033
-
 Benzyloxycarbonyl-Asp-Phe methyl ester pH 5.5 Bacillus thermoproteolyticus
0.059
-
 Benzyloxycarbonyl-Asp-Phe methyl ester pH 6.0 Bacillus thermoproteolyticus
0.076
-
 Benzyloxycarbonyl-Asp-Phe methyl ester pH 5.0 Bacillus thermoproteolyticus
2.8
-
 Benzyloxycarbonyl-Asp pH 5.0 or pH 6.0 Bacillus thermoproteolyticus

Organism

Organism UniProt Comment Textmining
Bacillus thermoproteolyticus
-
 commercial available thermolysin
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
benzyloxycarbonyl-Asp + Phe-methylester
-
 Bacillus thermoproteolyticus benzyloxycarbonyl-Asp-Phe methyl ester + H2O
-
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