| http://purl.uniprot.org/citations/3691501 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/3691501 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/3691501 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Citation |
| http://purl.uniprot.org/citations/3691501 | http://www.w3.org/2000/01/rdf-schema#comment | "1. The (R)-2-hydroxyglutaryl-CoA dehydratase system from Acidaminococcus fermentans was separated by chromatography of cell-free extracts on Q-Sepharose into two components, an activator and the actual dehydratase. The latter enzyme was further purified to homogeneity by chromatography on blue-Sepharose. It is an iron-sulfur protein (Mr 210,000) consisting of two different polypeptides (alpha, Mr 55,000, and beta, Mr 42,000) in an alpha 2 beta 2 structure with probably two [4Fe-4S] centers. After activation this purified enzyme catalysed the dehydration of (R)-2-hydroxyglutarate only in the presence of acetyl-CoA and glutaconate CoA-transferase, demonstrating that the thiol ester and not the free acid is the substrate of the dehydration. The result led to a modification of the hydroxyglutarate pathway of glutamate fermentation. 2. The activation of the dehydratase by the flow-through from Q-Sepharose concentrated by ultrafiltration required NADH, MgCl2, ATP and strict anaerobic conditions. This fraction was designated as Ao. Later when the concentration was performed by chromatography on phenyl-Sepharose, an NADH-independent form of the activator, designated as A*, was obtained. This enzyme, which required only ATP for activation of the dehydratase, was purified further by affinity chromatography on ATP-agarose. It contains neither iron nor inorganic sulfur. A*, as well as the activated dehydratase, were irreversibly inactivated by exposure to air within less than 15 min. The activated dehydratase but not A* was also inactivated by 1 mM hydroxylamine or by 0.1 mM 2,4-dinitrophenol. 3. The (R)-2-hydroxyglutaryl-CoA dehydratase system is closely related the that of (R)-lactoyl-CoA dehydratase from Clostridium propionicum as described by R. D. Kuchta and R. H. Abeles [(1985) J. Biol. Chem. 260, 13,181-13,189]."xsd:string |
| http://purl.uniprot.org/citations/3691501 | http://purl.org/dc/terms/identifier | "doi:10.1111/j.1432-1033.1987.tb13631.x"xsd:string |
| http://purl.uniprot.org/citations/3691501 | http://purl.org/dc/terms/identifier | "doi:10.1111/j.1432-1033.1987.tb13631.x"xsd:string |
| http://purl.uniprot.org/citations/3691501 | http://purl.uniprot.org/core/author | "Buckel W."xsd:string |
| http://purl.uniprot.org/citations/3691501 | http://purl.uniprot.org/core/author | "Buckel W."xsd:string |
| http://purl.uniprot.org/citations/3691501 | http://purl.uniprot.org/core/author | "Dutscho R."xsd:string |
| http://purl.uniprot.org/citations/3691501 | http://purl.uniprot.org/core/author | "Dutscho R."xsd:string |
| http://purl.uniprot.org/citations/3691501 | http://purl.uniprot.org/core/author | "Schweiger G."xsd:string |
| http://purl.uniprot.org/citations/3691501 | http://purl.uniprot.org/core/author | "Schweiger G."xsd:string |
| http://purl.uniprot.org/citations/3691501 | http://purl.uniprot.org/core/date | "1987"xsd:gYear |
| http://purl.uniprot.org/citations/3691501 | http://purl.uniprot.org/core/date | "1987"xsd:gYear |
| http://purl.uniprot.org/citations/3691501 | http://purl.uniprot.org/core/name | "Eur. J. Biochem."xsd:string |
| http://purl.uniprot.org/citations/3691501 | http://purl.uniprot.org/core/name | "Eur. J. Biochem."xsd:string |
| http://purl.uniprot.org/citations/3691501 | http://purl.uniprot.org/core/pages | "441-448"xsd:string |
| http://purl.uniprot.org/citations/3691501 | http://purl.uniprot.org/core/pages | "441-448"xsd:string |
| http://purl.uniprot.org/citations/3691501 | http://purl.uniprot.org/core/title | "Purification of 2-hydroxyglutaryl-CoA dehydratase from Acidaminococcus fermentans. An iron-sulfur protein."xsd:string |
| http://purl.uniprot.org/citations/3691501 | http://purl.uniprot.org/core/title | "Purification of 2-hydroxyglutaryl-CoA dehydratase from Acidaminococcus fermentans. An iron-sulfur protein."xsd:string |
| http://purl.uniprot.org/citations/3691501 | http://purl.uniprot.org/core/volume | "169"xsd:string |
| http://purl.uniprot.org/citations/3691501 | http://purl.uniprot.org/core/volume | "169"xsd:string |
| http://purl.uniprot.org/citations/3691501 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/3691501 |
| http://purl.uniprot.org/citations/3691501 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/3691501 |
| http://purl.uniprot.org/citations/3691501 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/3691501 |