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Isolation of an L ‐Stereospecific N ‐Acyl‐ L ‐proline‐Acylase and its Use as Catalyst in Organic Synthesis
Author(s) -
Groeger Ulrich,
Drauz Karlheinz,
Klenk Herbert
Publication year - 1990
Publication title -
angewandte chemie international edition in english
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 0570-0833
DOI - 10.1002/anie.199004171
Subject(s) - stereospecificity , proline , comamonas testosteroni , chemistry , enzyme , hydrolysis , bacteria , stereochemistry , catalysis , biochemistry , organic chemistry , amino acid , biology , genetics
Microbiological screening has resulted in the selection of the microorganism Comamonas testosteroni . Growth of this bacterium in the presence of N ‐acetyl‐ L ‐proline leads to formation of the enzyme N ‐acyl‐ L ‐proline acylase. The enzyme (molecular weight 380 ± 40 kDa, with eight identical subunits),is thermally stable to 70 °C. At pH values between 5 and 10 the enzyme causes stereospecific hydrolysis of N ‐acetyl‐ L ‐proline, making it useful for the resolution of racemic D,L ‐proline mixtures.