Protease-catalyzed synthesis of new hydrophobic dipeptides containing non-proteinogenic amino acids

Several dipeptides containing nonproteinogenic amino acids (especially l-tertiary leucine or l-neopentyglycine) were synthesized enzymatically. Thermolysin was used in solid-to-solid conversions in an equilibrium-controlled reaction while α-chymotrypsin was applied in kinetically controlled synthesi...

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Published inEnzyme and microbial technology Vol. 21; no. 4; pp. 252 - 257
Main Authors Krix, G., Eichhorn, U., Jakubke, H.-D., Kula, M.-R.
Format Journal Article
LanguageEnglish
Published Amsterdam Elsevier Inc 01.09.1997
Elsevier Science
Subjects
Bioconversions. Hemisynthesis
Biological and medical sciences
Biotechnology
enzymatic chymotrypsin
Fundamental and applied biological sciences. Psychology
Methods. Procedures. Technologies
neopentylglycin
Peptide synthesis
tertiary leucine
thermolysin
thermolysin
neopentylglycin
Peptide synthesis
enzymatic chymotrypsin
tertiary leucine
Enzymatic synthesis
Peptidases
Chymotrypsin
α-Aminoacid
Serine endopeptidases
Enzyme
Dipeptides
Hydrolases
Metalloendopeptidases
Thermolysin
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Summary:Several dipeptides containing nonproteinogenic amino acids (especially l-tertiary leucine or l-neopentyglycine) were synthesized enzymatically. Thermolysin was used in solid-to-solid conversions in an equilibrium-controlled reaction while α-chymotrypsin was applied in kinetically controlled synthesis. The dipeptide Z-Npg-Npg-NH 2 could be obtained using a protease mixture from Streptomyces. The active enzyme has not yet been purified.
ISSN:0141-0229
1879-0909
DOI:10.1016/S0141-0229(97)00037-9