| Predicate |
Object |
| assignee |
http://rdf.ncbi.nlm.nih.gov/pubchem/patentassignee/MD5_a31ec2a55659cd51c1d7fd639e328e21
http://rdf.ncbi.nlm.nih.gov/pubchem/patentassignee/MD5_1988bebce1678c5f3846465b3a584d7c |
| classificationCPCAdditional |
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/Y02E50-10
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/Y02P20-582 |
| classificationCPCInventive |
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12P7-24
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12N9-0006
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12P7-26
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12P7-16
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12P7-18
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12P41-002
http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12P7-04 |
| classificationIPCAdditional |
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12Q1-32
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12P21-00 |
| classificationIPCInventive |
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N9-04
http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C07K14-00 |
| filingDate |
2011-03-25-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| grantDate |
2013-07-02-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| inventor |
http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_257d98b25ecb29d998195254c4b2e452
http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_034a6ceb37369263b4798853cb1d0db2 |
| publicationDate |
2013-07-02-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| publicationNumber |
US-8476051-B2 |
| titleOfInvention |
Thermostable alcohol dehydrogenase derived from Thermococcus guaymasensis |
| abstract |
An alcohol dehydrogenase (ADH) from hyperthermophilic archaeon Thermococcus guaymasensis was purified to homogeneity and was found to be a homotetramer with a subunit size of 40±1 kDa. The gene encoding the enzyme was cloned and sequenced, and found to have significant sequence homology to known zinc-containing ADHs and L-threonine dehydrogenases with both binding motifs of catalytic zinc and NADP + . The wild-type enzyme is a primary-secondary ADH that exhibits a substrate preference for secondary alcohols and corresponding ketones, and exhibits unusual stereoselectivity. The wild-type enzyme was found to have outstanding thermostability, demonstrating 60% activity after incubation at 80° C. for 40 hours. Site-directed mutagenesis was used to substitute the cyteine residue at position 56 with a serine, to provide the TgADH(C56S) mutant. In the assays that we carried out, we found virtually no difference in enzyme activity and oxygen-sensitivity between the mutant TgADH (C56S) and wild type TgADH. |
| isCitedBy |
http://rdf.ncbi.nlm.nih.gov/pubchem/patent/US-11414962-B2 |
| priorityDate |
2008-09-26-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| type |
http://data.epo.org/linked-data/def/patent/Publication |