| http://purl.uniprot.org/citations/10940051 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/10940051 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/10940051 | http://www.w3.org/2000/01/rdf-schema#comment | "Two putative Methanococcus jannaschii isocitrate dehydrogenase genes, MJ1596 and MJ0720, were cloned and overexpressed in Escherichia coli, and their gene products were tested for the ability to catalyze the NAD- and NADP-dependent oxidative decarboxylation of DL-threo-3-isopropylmalic acid, threo-isocitrate, erythro-isocitrate, and homologs of threo-isocitrate. Neither enzyme was found to use any of the isomers of isocitrate as a substrate. The protein product of the MJ1596 gene, designated AksF, catalyzed the NAD-dependent decarboxylation of intermediates in the biosynthesis of 7-mercaptoheptanoic acid, a moiety of methanoarchaeal coenzyme B (7-mercaptoheptanylthreonine phosphate). These intermediates included (-)-threo-isohomocitrate [(-)-threo-1-hydroxy-1,2, 4-butanetricarboxylic acid], (-)-threo-iso(homo)(2)citrate [(-)-threo-1-hydroxy-1,2,5-pentanetricarboxylic acid], and (-)-threo-iso(homo)(3)citrate [(-)-threo-1-hydroxy-1,2, 6-hexanetricarboxylic acid]. The protein product of MJ0720 was found to be alpha-isopropylmalate dehydrogenase (LeuB) and was found to catalyze the NAD-dependent decarboxylation of one isomer of DL-threo-isopropylmalate to 2-ketoisocaproate; thus, it is involved in the biosynthesis of leucine. The AksF enzyme proved to be thermostable, losing only 10% of its enzymatic activity after heating at 100 degrees C for 10 min, whereas the LeuB enzyme lost 50% of its enzymatic activity after heating at 80 degrees C for 10 min."xsd:string |
| http://purl.uniprot.org/citations/10940051 | http://purl.org/dc/terms/identifier | "doi:10.1128/jb.182.17.5013-5016.2000"xsd:string |
| http://purl.uniprot.org/citations/10940051 | http://purl.org/dc/terms/identifier | "doi:10.1128/jb.182.17.5013-5016.2000"xsd:string |
| http://purl.uniprot.org/citations/10940051 | http://purl.uniprot.org/core/author | "White R.H."xsd:string |
| http://purl.uniprot.org/citations/10940051 | http://purl.uniprot.org/core/author | "White R.H."xsd:string |
| http://purl.uniprot.org/citations/10940051 | http://purl.uniprot.org/core/author | "Xu H."xsd:string |
| http://purl.uniprot.org/citations/10940051 | http://purl.uniprot.org/core/author | "Xu H."xsd:string |
| http://purl.uniprot.org/citations/10940051 | http://purl.uniprot.org/core/author | "Graupner M."xsd:string |
| http://purl.uniprot.org/citations/10940051 | http://purl.uniprot.org/core/author | "Graupner M."xsd:string |
| http://purl.uniprot.org/citations/10940051 | http://purl.uniprot.org/core/author | "Howell D.M."xsd:string |
| http://purl.uniprot.org/citations/10940051 | http://purl.uniprot.org/core/author | "Howell D.M."xsd:string |
| http://purl.uniprot.org/citations/10940051 | http://purl.uniprot.org/core/date | "2000"xsd:gYear |
| http://purl.uniprot.org/citations/10940051 | http://purl.uniprot.org/core/date | "2000"xsd:gYear |
| http://purl.uniprot.org/citations/10940051 | http://purl.uniprot.org/core/name | "J. Bacteriol."xsd:string |
| http://purl.uniprot.org/citations/10940051 | http://purl.uniprot.org/core/name | "J. Bacteriol."xsd:string |
| http://purl.uniprot.org/citations/10940051 | http://purl.uniprot.org/core/pages | "5013-5016"xsd:string |
| http://purl.uniprot.org/citations/10940051 | http://purl.uniprot.org/core/pages | "5013-5016"xsd:string |
| http://purl.uniprot.org/citations/10940051 | http://purl.uniprot.org/core/title | "Identification of enzymes homologous to isocitrate dehydrogenase that are involved in coenzyme B and leucine biosynthesis in methanoarchaea."xsd:string |
| http://purl.uniprot.org/citations/10940051 | http://purl.uniprot.org/core/title | "Identification of enzymes homologous to isocitrate dehydrogenase that are involved in coenzyme B and leucine biosynthesis in methanoarchaea."xsd:string |
| http://purl.uniprot.org/citations/10940051 | http://purl.uniprot.org/core/volume | "182"xsd:string |
| http://purl.uniprot.org/citations/10940051 | http://purl.uniprot.org/core/volume | "182"xsd:string |
| http://purl.uniprot.org/citations/10940051 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/10940051 |
| http://purl.uniprot.org/citations/10940051 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/10940051 |