http://rdf.ncbi.nlm.nih.gov/pubchem/patent/CN-109295028-B
Outgoing Links
Predicate | Object |
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classificationCPCInventive | http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12Y207-02004 http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12N9-1217 http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12N15-70 |
classificationIPCInventive | http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N1-21 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N9-12 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N15-70 |
filingDate | 2018-11-05-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
grantDate | 2021-12-17-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
publicationDate | 2021-12-17-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
publicationNumber | CN-109295028-B |
titleOfInvention | High-enzyme-activity aspartokinase mutant, engineering bacterium and preparation method of mutant |
abstract | An aspartokinase mutant, engineering bacteria and a preparation method of the mutant belong to the technical field of biological engineering. The high-enzyme-activity aspartokinase mutant is a sequence formed by substituting, deleting or adding 2-10, further 2-6 and further 2-3 amino acid residues of exogenous aspartokinase with an amino acid sequence shown as SEQ ID NO. 2, and has the function of aspartokinase. The sequence is preferably formed by substituting, deleting or adding 2 amino acid residues, particularly preferably, the amino acid at the 372 nd position and the 379 th position in the amino acid sequence is subjected to site-directed saturation mutation, and the high-enzyme-activity aspartokinase mutant is selected by using a high-throughput screening method. The invention further utilizes an electric conversion method to transfer the pEC-AK recombinant shuttle expression vector of the aspartokinase mutant with high enzyme activity and the effect of relieving or weakening Lys feedback inhibition into the corynebacterium beijing, finally obtains the recombinant corynebacterium beijing M372I-T379S engineering bacteria, and carries out fermentation product analysis on the engineering bacteria. |
priorityDate | 2018-11-05-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
type | http://data.epo.org/linked-data/def/patent/Publication |
Incoming Links
Total number of triples: 287.