http://rdf.ncbi.nlm.nih.gov/pubchem/patent/CN-106676084-B

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classificationCPCInventive http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12P41-005
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12Y301-01003
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12P13-002
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12N9-20
classificationIPCInventive http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12P41-00
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N9-20
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http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12P13-00
filingDate 2017-02-09-04:00^^<http://www.w3.org/2001/XMLSchema#date>
grantDate 2019-11-29-04:00^^<http://www.w3.org/2001/XMLSchema#date>
publicationDate 2019-11-29-04:00^^<http://www.w3.org/2001/XMLSchema#date>
publicationNumber CN-106676084-B
titleOfInvention A lipase mutant derived from Talaromyces thermophilus, its encoding gene and its application
abstract The invention discloses a lipase mutant derived from Talaromyces thermophilus, an encoding gene and the synthesis of ethyl 2-carboxyethyl-3-cyano-5-methylhexanoate by hydrolysis (3S )-2-carboxyethyl-3-cyano-5-methylhexanoic acid, the mutant is the 206th, 207th and 259th amino acids of the amino acid sequence shown in SEQ ID No.1. obtained by mutating one or more of the positions. After protein molecular modification, the activity of TTL stereoselective hydrolysis of CNDE was increased from 4.50U/mg to 160.55U/mg, which was much higher than the reported activity of lipase to hydrolyze CNDE. Therefore, the mutant obtained by the present invention has a good application prospect in the efficient catalysis of CNDE to synthesize pregabalin chiral intermediate (3S)-2-carboxyethyl-3-cyano-5-methylhexanoic acid.
priorityDate 2017-02-09-04:00^^<http://www.w3.org/2001/XMLSchema#date>
type http://data.epo.org/linked-data/def/patent/Publication

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