| http://purl.uniprot.org/citations/112095 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/112095 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/112095 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Citation |
| http://purl.uniprot.org/citations/112095 | http://www.w3.org/2000/01/rdf-schema#comment | "Inositol 2-dehydrogenase (EC 1.1.1.18) activity appears during growth of Bacillus subtilis (strain 60015) in nutrient sporulation medium. Its synthesis is induced by myo-inositol and repressed by D-glucose. The enzyme has an apparent molecular weight of 155,000 to 160,000 as determined by sucrose density gradient centrifugation, and it is comprised of four subunits, each having a molecular weight of 39,000 as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The isoelectric point of the enzyme is 4.4 as determined by column isoelectric focusing. The enzyme shows the highest Vmax and lowest Km with myo-inositol as substrate but does not react with scyllo-inositol; it also reacts with the alpha anomer (but not the beta anomer) of D-glucose and with D-xylose. Apparently, the enzyme can remove only the single equatorial hydrogen of the cyclitol or pyranose ring. In contrast to the glucose dehydrogenase of spores, which reacts with D-glucose or 2-deoxy-D-glucose and with NAD or NADP, inositol dehydrogenase requires NAD and does not react with 2-deoxy-D-glucose."xsd:string |
| http://purl.uniprot.org/citations/112095 | http://purl.org/dc/terms/identifier | "doi:10.1016/s0021-9258(18)36000-9"xsd:string |
| http://purl.uniprot.org/citations/112095 | http://purl.org/dc/terms/identifier | "doi:10.1016/s0021-9258(18)36000-9"xsd:string |
| http://purl.uniprot.org/citations/112095 | http://purl.uniprot.org/core/author | "Fujita Y."xsd:string |
| http://purl.uniprot.org/citations/112095 | http://purl.uniprot.org/core/author | "Fujita Y."xsd:string |
| http://purl.uniprot.org/citations/112095 | http://purl.uniprot.org/core/author | "Freese E."xsd:string |
| http://purl.uniprot.org/citations/112095 | http://purl.uniprot.org/core/author | "Freese E."xsd:string |
| http://purl.uniprot.org/citations/112095 | http://purl.uniprot.org/core/author | "Ramaley R."xsd:string |
| http://purl.uniprot.org/citations/112095 | http://purl.uniprot.org/core/author | "Ramaley R."xsd:string |
| http://purl.uniprot.org/citations/112095 | http://purl.uniprot.org/core/date | "1979"xsd:gYear |
| http://purl.uniprot.org/citations/112095 | http://purl.uniprot.org/core/date | "1979"xsd:gYear |
| http://purl.uniprot.org/citations/112095 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/112095 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/112095 | http://purl.uniprot.org/core/pages | "7684-7690"xsd:string |
| http://purl.uniprot.org/citations/112095 | http://purl.uniprot.org/core/pages | "7684-7690"xsd:string |
| http://purl.uniprot.org/citations/112095 | http://purl.uniprot.org/core/title | "Purification and properties of Bacillus subtilis inositol dehydrogenase."xsd:string |
| http://purl.uniprot.org/citations/112095 | http://purl.uniprot.org/core/title | "Purification and properties of Bacillus subtilis inositol dehydrogenase."xsd:string |
| http://purl.uniprot.org/citations/112095 | http://purl.uniprot.org/core/volume | "254"xsd:string |
| http://purl.uniprot.org/citations/112095 | http://purl.uniprot.org/core/volume | "254"xsd:string |
| http://purl.uniprot.org/citations/112095 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/112095 |
| http://purl.uniprot.org/citations/112095 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/112095 |
| http://purl.uniprot.org/citations/112095 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/112095 |