Premium
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.
Accelerating Research
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom
Address
John Eccles HouseRobert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom