| Predicate |
Object |
| classificationCPCAdditional |
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12Y401-01033 |
| classificationCPCInventive |
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12N15-52
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12N15-743
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12N15-09
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12P5-007
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12P5-02
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12P5-026
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12N5-10
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12P21-02
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12N15-8257
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12N9-88
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12N15-70
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12Y401-01033
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12N15-8205 |
| classificationIPCInventive |
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N9-88
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N15-09
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12P5-02
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12P21-02
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N1-21
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N1-19
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N1-15
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N5-10 |
| filingDate |
2017-09-26-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| grantDate |
2022-11-29-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| publicationDate |
2022-11-29-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| publicationNumber |
CN-109715815-B |
| titleOfInvention |
Diphosphomevalonate decarboxylase variant and method for producing olefin compound using the variant |
| abstract |
The present invention introduces mutations accompanied by amino acid substitutions into various parts of diphosphomevalonate decarboxylase (MVD), and prepares various variants of MVD. Then, as a result of evaluating the catalytic activity for the production of olefin compounds such as isoprene with respect to the variant, it was found that the catalytic activity was improved by replacing glycine at position 152 with another amino acid. It was also shown that MVD in which arginine at position 74 and threonine at position 209 were each replaced with other amino acids in addition to position 152 also had the above-mentioned high catalytic activity. |
| priorityDate |
2016-09-28-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| type |
http://data.epo.org/linked-data/def/patent/Publication |