| http://purl.uniprot.org/citations/11422389 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/11422389 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/11422389 | http://www.w3.org/2000/01/rdf-schema#comment | "In Escherichia coli and Aspergillus nidulans, propionate is oxidized to pyruvate via the methylcitrate cycle. The last step of this cycle, the cleavage of 2-methylisocitrate to succinate and pyruvate is catalysed by 2-methylisocitrate lyase. The enzymes from both organisms were assayed with chemically synthesized threo-2-methylisocitrate; the erythro-diastereomer was not active. 2-Methylisocitrate lyase from E. coli corresponds to the PrpB protein of the prp operon involved in propionate oxidation. The purified enzyme has a molecular mass of approximately 32 kDa per subunit, which is lower than those of isocitrate lyases from bacterial sources ( approximately 48 kDa). 2-Methylisocitrate lyase from A. nidulans shows an apparent molecular mass of 66 kDa per subunit, almost equal to that of isocitrate lyase of the same organism. Both 2-methylisocitrate lyases have a native homotetrameric structure as identified by size-exclusion chromatography. The enzymes show no measurable activity with isocitrate. Starting from 250 mM pyruvate, 150 mM succinate and 10 microM PrpB, the enzymatically active stereoisomer could be synthesized in 1% yield. As revealed by chiral HPLC, the product consisted of a single enantiomer. This isomer is cleaved by 2-methylisocitrate lyases from A. nidulans and E. coli. The PrpB protein reacted with stoichiometric amounts of 3-bromopyruvate whereby the activity was lost and one amino-acid residue per subunit became modified, most likely a cysteine as shown for isocitrate lyase of E. coli. PrpB exhibits 34% sequence identity with carboxyphosphoenolpyruvate phosphonomutase from Streptomyces hygroscopicus, in which the essential cysteine residue is conserved."xsd:string |
| http://purl.uniprot.org/citations/11422389 | http://purl.org/dc/terms/identifier | "doi:10.1046/j.1432-1327.2001.02262.x"xsd:string |
| http://purl.uniprot.org/citations/11422389 | http://purl.org/dc/terms/identifier | "doi:10.1046/j.1432-1327.2001.02262.x"xsd:string |
| http://purl.uniprot.org/citations/11422389 | http://purl.uniprot.org/core/author | "Buckel W."xsd:string |
| http://purl.uniprot.org/citations/11422389 | http://purl.uniprot.org/core/author | "Buckel W."xsd:string |
| http://purl.uniprot.org/citations/11422389 | http://purl.uniprot.org/core/author | "Brock M."xsd:string |
| http://purl.uniprot.org/citations/11422389 | http://purl.uniprot.org/core/author | "Brock M."xsd:string |
| http://purl.uniprot.org/citations/11422389 | http://purl.uniprot.org/core/author | "Darley D."xsd:string |
| http://purl.uniprot.org/citations/11422389 | http://purl.uniprot.org/core/author | "Darley D."xsd:string |
| http://purl.uniprot.org/citations/11422389 | http://purl.uniprot.org/core/author | "Textor S."xsd:string |
| http://purl.uniprot.org/citations/11422389 | http://purl.uniprot.org/core/author | "Textor S."xsd:string |
| http://purl.uniprot.org/citations/11422389 | http://purl.uniprot.org/core/date | "2001"xsd:gYear |
| http://purl.uniprot.org/citations/11422389 | http://purl.uniprot.org/core/date | "2001"xsd:gYear |
| http://purl.uniprot.org/citations/11422389 | http://purl.uniprot.org/core/name | "Eur. J. Biochem."xsd:string |
| http://purl.uniprot.org/citations/11422389 | http://purl.uniprot.org/core/name | "Eur. J. Biochem."xsd:string |
| http://purl.uniprot.org/citations/11422389 | http://purl.uniprot.org/core/pages | "3577-3586"xsd:string |
| http://purl.uniprot.org/citations/11422389 | http://purl.uniprot.org/core/pages | "3577-3586"xsd:string |
| http://purl.uniprot.org/citations/11422389 | http://purl.uniprot.org/core/title | "2-Methylisocitrate lyases from the bacterium Escherichia coli and the filamentous fungus Aspergillus nidulans: characterization and comparison of both enzymes."xsd:string |
| http://purl.uniprot.org/citations/11422389 | http://purl.uniprot.org/core/title | "2-Methylisocitrate lyases from the bacterium Escherichia coli and the filamentous fungus Aspergillus nidulans: characterization and comparison of both enzymes."xsd:string |
| http://purl.uniprot.org/citations/11422389 | http://purl.uniprot.org/core/volume | "268"xsd:string |
| http://purl.uniprot.org/citations/11422389 | http://purl.uniprot.org/core/volume | "268"xsd:string |
| http://purl.uniprot.org/citations/11422389 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/11422389 |
| http://purl.uniprot.org/citations/11422389 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/11422389 |