| http://purl.uniprot.org/citations/7826335 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/7826335 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/7826335 | http://www.w3.org/2000/01/rdf-schema#comment | "Cysteine-195 was previously identified as a probable active site residue in isocitrate lyase (ICL) from Escherichia coli ML308 [Nimmo, Douglas, Kleanthous, Campbell and MacKintosh (1989) Biochem. J. 261, 431-435]. This residue was replaced with serine and alanine residues by site-directed mutagenesis. The mutated genes expressed proteins with low but finite ICL activity, which co-migrated with wild-type ICL on both SDS/ and native PAGE. The mutant proteins were purified and characterized. Fluorimetry and c.d. in both the near- and the far-u.v. regions showed no differences between the mutants and wild-type ICL, indicating that the conformations of the three enzymes were very similar. ICL C195A (Cys-195-->Ala) and C195S (Cys-195-->Ser) showed 8.4-fold and 3.6-fold increases in the Km for isocitrate, while their kcat. values showed 30- and 100-fold decreases respectively. The effect of pH on the kinetic properties of the wild-type and mutant ICLs was investigated. The results showed that the response of the mutant enzymes to pH was simpler than that of the wild-type. For the mutants, ionisation of a group with a pKa of approx. 7.8 affected the Km for isocitrate and kcat.. For the wild-type enzyme, these parameters were affected by the ionization of two or more groups, one of which is presumed to by cysteine-195. The results are consistent with the view that the previously identified group with a pKa of 7.1 whose ionization affects the reaction of ICL by iodoacetate is cysteine-195 itself."xsd:string |
| http://purl.uniprot.org/citations/7826335 | http://purl.org/dc/terms/identifier | "doi:10.1042/bj3050239"xsd:string |
| http://purl.uniprot.org/citations/7826335 | http://purl.org/dc/terms/identifier | "doi:10.1042/bj3050239"xsd:string |
| http://purl.uniprot.org/citations/7826335 | http://purl.uniprot.org/core/author | "Robertson A.G."xsd:string |
| http://purl.uniprot.org/citations/7826335 | http://purl.uniprot.org/core/author | "Robertson A.G."xsd:string |
| http://purl.uniprot.org/citations/7826335 | http://purl.uniprot.org/core/author | "Nimmo H.G."xsd:string |
| http://purl.uniprot.org/citations/7826335 | http://purl.uniprot.org/core/author | "Nimmo H.G."xsd:string |
| http://purl.uniprot.org/citations/7826335 | http://purl.uniprot.org/core/date | "1995"xsd:gYear |
| http://purl.uniprot.org/citations/7826335 | http://purl.uniprot.org/core/date | "1995"xsd:gYear |
| http://purl.uniprot.org/citations/7826335 | http://purl.uniprot.org/core/name | "Biochem. J."xsd:string |
| http://purl.uniprot.org/citations/7826335 | http://purl.uniprot.org/core/name | "Biochem. J."xsd:string |
| http://purl.uniprot.org/citations/7826335 | http://purl.uniprot.org/core/pages | "239-244"xsd:string |
| http://purl.uniprot.org/citations/7826335 | http://purl.uniprot.org/core/pages | "239-244"xsd:string |
| http://purl.uniprot.org/citations/7826335 | http://purl.uniprot.org/core/title | "Site-directed mutagenesis of cysteine-195 in isocitrate lyase from Escherichia coli ML308."xsd:string |
| http://purl.uniprot.org/citations/7826335 | http://purl.uniprot.org/core/title | "Site-directed mutagenesis of cysteine-195 in isocitrate lyase from Escherichia coli ML308."xsd:string |
| http://purl.uniprot.org/citations/7826335 | http://purl.uniprot.org/core/volume | "305"xsd:string |
| http://purl.uniprot.org/citations/7826335 | http://purl.uniprot.org/core/volume | "305"xsd:string |
| http://purl.uniprot.org/citations/7826335 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/7826335 |
| http://purl.uniprot.org/citations/7826335 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/7826335 |
| http://purl.uniprot.org/citations/7826335 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/7826335 |
| http://purl.uniprot.org/citations/7826335 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/7826335 |
| http://purl.uniprot.org/uniprot/P0A9G6 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/7826335 |
| http://purl.uniprot.org/uniprot/P0A9G6#attribution-AECC329466ED18899E22E43348BDCA28 | http://purl.uniprot.org/core/source | http://purl.uniprot.org/citations/7826335 |