| Predicate |
Object |
| assignee |
http://rdf.ncbi.nlm.nih.gov/pubchem/patentassignee/MD5_f60f7884c3b8246b6939e7ca6e98d356 |
| classificationCPCInventive |
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12P21-06
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12N9-80 |
| classificationIPCAdditional |
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12R1-19
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12R1-01 |
| classificationIPCInventive |
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N9-48
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N15-09
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N9-78
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N15-00
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12Q1-34
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N1-21
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N1-20
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C07H21-04
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C07H21-02
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C07K16-40
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N9-80
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12P21-08
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12P21-06 |
| filingDate |
1997-10-15-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| grantDate |
2000-10-24-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| inventor |
http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_ad68fab584553695f455614bcf548f72
http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_223f19bea9c5b09001db7e1a4e91350f
http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_50f63f3a35101fc1a5f20222e358c4b9 |
| publicationDate |
2000-10-24-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| publicationNumber |
US-6136583-A |
| titleOfInvention |
Amidase |
| abstract |
A purified thermostable enzyme is derived from the archael bacterium Thermococcus GU5L5. The enzyme has a molecular weight of about 68.5 kilodaltons and has cellulase activity. The enzyme can be produced from native or recombinant host cells and can be used for the removal of arginine, phenylalanine, or methionine amino acids from the N-terminal end of peptides in peptide or peptidomimetic synthesis. The enzyme is selective for the L, or 'natural' enantiomer of the amino acid derivatives and is therefore useful for the production of optically active compounds. These reactions can be performed in the presence of the chemically more reactive ester functionality, a step which is very difficult to achieve with nonenzymatic methods. |
| isCitedBy |
http://rdf.ncbi.nlm.nih.gov/pubchem/patent/US-6500659-B1 |
| priorityDate |
1996-06-17-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| type |
http://data.epo.org/linked-data/def/patent/Publication |