| http://purl.uniprot.org/citations/6954878 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/6954878 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/6954878 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Citation |
| http://purl.uniprot.org/citations/6954878 | http://www.w3.org/2000/01/rdf-schema#comment | "Peptostreptococcus productus strain b-52 (a human fecal isolate) and Eubacterium aerofaciens ATCC 25986 were found to contain NADP-dependent 7 beta-hydroxysteriod dehydrogenase activity. The enzyme was synthesized constitutively by both organisms, and the enzyme yields were suppressed by the addition of 0.5 mM 7 beta-hydroxy bile acid to the growth medium. Purification of the enzyme by chromatography resulted in preparations with 3.5 (P. productus b-52, on Sephadex G-200) and 1.8 (E. aerofaciens, on Bio-Gel A-1.5 M) times the activity of the crude cell extracts. A pH optimum of 9.8 and a molecular weight of approximately 53,000 were shown for the enzyme of strain b-52, and an optimum pH at 10.5 and a molecular weight of 45,000 was shown for that from strain ATCC 25986. Kinetic studies revealed that both enzyme preparations oxidized the 7 beta-hydroxy group in unconjugated and conjugated bile acids, a lower Km value being demonstrated with free bile acid than with glycine and taurine conjugates. No measureable activity against 3 alpha-, 7 alpha-, or 12 alpha-hydroxy groups was detected in either enzyme preparation. When tested with strain ATCC 25986, little 7 beta-hydroxy-steroid dehydrogenase activity was detected in cells grown in the presence of glucose in excess. The enzyme from strain b-52 was found to be heat labile (90% inactivation at 50 degrees C for 3 min) and highly sensitive to sulfhydryl inhibitors."xsd:string |
| http://purl.uniprot.org/citations/6954878 | http://purl.org/dc/terms/identifier | "doi:10.1128/aem.43.5.1057-1063.1982"xsd:string |
| http://purl.uniprot.org/citations/6954878 | http://purl.org/dc/terms/identifier | "doi:10.1128/aem.43.5.1057-1063.1982"xsd:string |
| http://purl.uniprot.org/citations/6954878 | http://purl.uniprot.org/core/author | "Hirano S."xsd:string |
| http://purl.uniprot.org/citations/6954878 | http://purl.uniprot.org/core/author | "Hirano S."xsd:string |
| http://purl.uniprot.org/citations/6954878 | http://purl.uniprot.org/core/author | "Masuda N."xsd:string |
| http://purl.uniprot.org/citations/6954878 | http://purl.uniprot.org/core/author | "Masuda N."xsd:string |
| http://purl.uniprot.org/citations/6954878 | http://purl.uniprot.org/core/date | "1982"xsd:gYear |
| http://purl.uniprot.org/citations/6954878 | http://purl.uniprot.org/core/date | "1982"xsd:gYear |
| http://purl.uniprot.org/citations/6954878 | http://purl.uniprot.org/core/name | "Appl. Environ. Microbiol."xsd:string |
| http://purl.uniprot.org/citations/6954878 | http://purl.uniprot.org/core/name | "Appl. Environ. Microbiol."xsd:string |
| http://purl.uniprot.org/citations/6954878 | http://purl.uniprot.org/core/pages | "1057-1063"xsd:string |
| http://purl.uniprot.org/citations/6954878 | http://purl.uniprot.org/core/pages | "1057-1063"xsd:string |
| http://purl.uniprot.org/citations/6954878 | http://purl.uniprot.org/core/title | "Characterization of NADP-dependent 7 beta-hydroxysteroid dehydrogenases from Peptostreptococcus productus and Eubacterium aerofaciens."xsd:string |
| http://purl.uniprot.org/citations/6954878 | http://purl.uniprot.org/core/title | "Characterization of NADP-dependent 7 beta-hydroxysteroid dehydrogenases from Peptostreptococcus productus and Eubacterium aerofaciens."xsd:string |
| http://purl.uniprot.org/citations/6954878 | http://purl.uniprot.org/core/volume | "43"xsd:string |
| http://purl.uniprot.org/citations/6954878 | http://purl.uniprot.org/core/volume | "43"xsd:string |
| http://purl.uniprot.org/citations/6954878 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/6954878 |
| http://purl.uniprot.org/citations/6954878 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/6954878 |
| http://purl.uniprot.org/citations/6954878 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/6954878 |
| http://purl.uniprot.org/citations/6954878 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/6954878 |
| http://purl.uniprot.org/citations/6954878 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/6954878 |