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Literature summary for 3.4.21.62 extracted from

  • Boeriu, C.; Frissen, A.; Boer, E.; Van Kekem, K.; Van Zoelen, D.; Eggen, I.
    Optimized enzymatic synthesis of C-terminal peptide amides using subtilisin A from Bacillus licheniformis (2010), J. Mol. Catal. B, 66, 33-42.
No PubMed abstract available

Organism

Organism UniProt Comment Textmining
Bacillus licheniformis
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Z-Ala-Phe-OMe + H2O enzymatic method for the synthesis of free terminal amides of peptides, by ammonolysis of peptide methyl esters using ammonium carbamate and subtilisin A from Bacillus licheniformis in polar organic solvents with low water content is developed. Enzyme is very stable and active in a mixture of t-BuOH and DMF 82.5:17.5 (v/v), containing 0.2% water. Optimum conditions for Z-Ala-Phe-NH2 synthesis are molar ratio ammonium carbamate to Z-Ala-Phe-OMe 10, in t-BuOH/DMF, 82.5:17.5 (v/v) containing 0.2% (v) water, at 30°C for 21 h with the maximum yield of 87% Bacillus licheniformis Z-Ala-Phe-NH2 + methanol
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Synonyms

Synonyms Comment Organism
subtilisin A
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Bacillus licheniformis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
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assay at Bacillus licheniformis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
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assay at Bacillus licheniformis