http://rdf.ncbi.nlm.nih.gov/pubchem/patent/JP-2006051034-A
Outgoing Links
| Predicate | Object |
|---|---|
| assignee | http://rdf.ncbi.nlm.nih.gov/pubchem/patentassignee/MD5_cebc9740ef706cde29e885504f274ffa |
| classificationIPCAdditional | http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12R1-01 |
| classificationIPCInventive | http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N9-80 http://rdf.ncbi.nlm.nih.gov/pubchem/patentipc/C12N15-09 |
| filingDate | 2005-09-05-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| inventor | http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_a1b0bf4220888ac5a98dafb54fd27c17 http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_f7bbb06c7f97df9f37e99b01dc41ace3 |
| publicationDate | 2006-02-23-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| publicationNumber | JP-2006051034-A |
| titleOfInvention | Novel amidase gene |
| abstract | The present invention provides a novel protein having amidase activity for stereoselectively hydrolyzing α-amino acid amide and α-hydroxy acid amide, and a gene encoding the protein. The protein comprises (a) a protein comprising an amino acid sequence represented by a specific sequence derived from Enterobacter cloassay, or (b) one or more of the amino acid sequences represented by the specific sequence. It is a protein having an amidase activity that includes an amino acid sequence in which an amino acid is deleted, substituted or added, and stereoselectively hydrolyzes an α-amino acid amide and an α-hydroxy acid amide. [Effect] Many amidase genes cloned by the gene recombination method can be present in the microbial cells, so that microorganisms with dramatically increased catalytic ability compared to conventional methods can be provided. -An optically active α-amino acid or α-hydroxy acid can be efficiently produced from an amino acid amide and an α-hydroxy acid amide. [Selection figure] None |
| priorityDate | 1999-04-16-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| type | http://data.epo.org/linked-data/def/patent/Publication |
Incoming Links
Total number of triples: 69.