http://rdf.ncbi.nlm.nih.gov/pubchem/patent/WO-2007145539-A2
Outgoing Links
| Predicate | Object |
|---|---|
| assignee | http://rdf.ncbi.nlm.nih.gov/pubchem/patentassignee/MD5_e2a2b434678e4f5d602f8fbc188276b8 http://rdf.ncbi.nlm.nih.gov/pubchem/patentassignee/MD5_0fc254160d7adc52cafa6b26e72f7fb1 http://rdf.ncbi.nlm.nih.gov/pubchem/patentassignee/MD5_5e87fce0c9bc2bf67ae4fa88e2684dc8 http://rdf.ncbi.nlm.nih.gov/pubchem/patentassignee/MD5_a458567abb7c020bb777aef4913958ee http://rdf.ncbi.nlm.nih.gov/pubchem/patentassignee/MD5_e1c35a4d0e269eaf0718f5adf7898267 http://rdf.ncbi.nlm.nih.gov/pubchem/patentassignee/MD5_15707ec0adc07c4136d58363d6f22da0 |
| classificationCPCInventive | http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12Y113-99001 http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/C12N9-0069 http://rdf.ncbi.nlm.nih.gov/pubchem/patentcpc/A61P3-10 |
| filingDate | 2007-06-14-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| inventor | http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_2c95981246f6657395d621774614fab9 http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_81011355d19653a7e0e5cf8fe44d5810 http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_f84893045f6ed85903548180251cceca http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_b09c74056446bfd3440d8a9077518ff0 http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_0dd1031e8681be82d48dc4a9cf2b4c40 http://rdf.ncbi.nlm.nih.gov/pubchem/patentinventor/MD5_570d85e52977491f1d21dfc8a22e1d6a |
| publicationDate | 2007-12-21-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| publicationNumber | WO-2007145539-A2 |
| titleOfInvention | Crystal structure of a substrate complex of miox |
| abstract | Diabetes mellitus is a chronic disease that is associated with altered metabolism of the inositol sugars myo-inositol (MI) and D-chiro-inositol (DCI). In animals, catabolism of MI and DCI depends on the enzyme myo-inositol oxygenase (MIOX), which catalyzes the first committed step of the glucuronate-xylulose pathway, and is found almost exclusively in the kidneys. The crystal structure of MIOX, in complex with MI, has been determined by multiwavelength anomalous diffraction methods and refined at 2.0-A resolution (R = 0.208, Rfree = 0.258). The structure reveals a monomeric, single-domain protein with a mostly-helical fold that is distantly related to the diverse HD domain superfamily. Five helices form the structural core and provide six ligands (4 His and 2 Asp) for the di-iron center, in which the two iron atoms are bridged by a putative hydroxide ion and one of the aspartate ligands, Asp124. A key loop forms a lid over the MI substrate, which is coordinated in bidentate mode to one iron atom. It is proposed that this mode of iron coordination, and interaction with a key lysine residue, activate MI for bond cleavage. The structure also reveals the basis of substrate specificity and suggests routes for the development of specific MIOX inhibitors for treatment of inositol-associated disorders. |
| priorityDate | 2006-06-14-04:00^^<http://www.w3.org/2001/XMLSchema#date> |
| type | http://data.epo.org/linked-data/def/patent/Publication |
Incoming Links
Total number of triples: 264.