| Predicate |
Object |
| assignee |
http://rdf.ncbi.nlm.nih.gov/pubchem/patentassignee/MD5_b828305495e1cdb63947a3a18aa633d1 |
| classificationCPCAdditional |
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/Y10S435-814 |
| classificationCPCInventive |
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12N15-8243
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12N15-52
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12P5-007
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12N9-90
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C08F136-08 |
| classificationIPCInventive |
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N9-90
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N5-10
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N15-82
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N15-61
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N15-29
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N15-09
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/C12P5-02 |
| filingDate |
1999-05-11-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| inventor |
http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_5e70ee5e4cc310eb6a64a94be2975fdb
http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_8491d69df15a80bfbc51aa92ad81317e
http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_0328c5708b08a887ca15e2095f2fc5ad
http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_32503965bffba0eed08e995ae2b12433
http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_3517b150badbacb1f900c222ca2812c5 |
| publicationDate |
2000-11-25-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| publicationNumber |
KR-20000067734-A |
| titleOfInvention |
Isopentenyl diphosphate isomerase from hevea brasiliensis and rubber producing method using the same |
| abstract |
The cDNA clones encoded by isopentenyl diphosphate (IPP) isomerase (EC 5.3.3.2) were cloned from the cDNA library of the latex of Hebraa brasiliensis. The clone has a continuous open reading frame encoded with a peptide of 234 amino acids with an expected molecular weight of 26.7 kDa. The deduced protein is acidic with an isoelectric point of 4.7 and shows high sequence identity with other IPP isomerases. Recombinant protein expressed in Escherichia coli exhibits IPP isomerase activity. Washed rubber particles (WRP) depleted of the initiator allyl diphosphate were used to add IPP isomerase to the reaction mixture and biosynthetic analysis of rubber in vitro was performed. It has been shown that recombinant IPP isomerase catalyzes the conversion of IPP to DMAPP, an important activation step of basic 5-carbon isoprene units in rubber biosynthesis. Southern analysis confirmed that the IPP isomerase is encoded by two genes from the Brazilian rubber tree. In Northern blot analysis, only one hybridizing band was detected from the fluid, while two transcripts of different sizes (1.2 kb and 0.6 kb) were detected from the leaf tissue. Analysis of the extracted milk of the nail wound tree and RNA extracted from the leaf tissue revealed that the wound did not alter the transcription level of IPP isomerase. |
| isCitedBy |
http://rdf.ncbi.nlm.nih.gov/pubchem/patent/WO-2016048061-A3 |
| priorityDate |
1999-04-22-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| type |
http://data.epo.org/linked-data/def/patent/Publication |