http://purl.uniprot.org/citations/3311744 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/3311744 | http://www.w3.org/2000/01/rdf-schema#comment | "The kinetic properties of Trypanosoma brucei brucei triose-phosphate isomerase are compared with those of the commercially available rabbit muscle and yeast enzymes and with published data on the chicken muscle enzyme. With glyceraldehyde 3-phosphate as substrate Km = 0.25 +/-0.05 mM and kcat = 3.7 X 10(5) min-1. With dihydroxyacetone phosphate as substrate Km = 1.2 +/-0.1 mM and kcat = 6.5 X 10(4) min-1. The pH dependence of Km and Vmax at 0.1 M ionic strength is in agreement with the results published for the yeast and chicken muscle enzymes. At ionic strength below 0.05 M the effect of a charged group specific for the trypanosomal enzyme and absent from the yeast and rabbit muscle enzymes becomes detectable. This effect significantly increases Km whereas Vmax becomes slightly higher. Trypanosomal triose-phosphate isomerase is inhibited by sulphate, phosphate and arsenate ions, by 2-phosphoglycolate and a number of documented inhibitors in the same concentration range as are the other triose-phosphate isomerases. The trypanocidal drug, Suramin inhibits T. brucei and rabbit muscle triose-phosphate isomerase to the same extent while leaving the yeast enzyme relatively unaffected."xsd:string |
http://purl.uniprot.org/citations/3311744 | http://purl.org/dc/terms/identifier | "doi:10.1111/j.1432-1033.1987.tb13388.x"xsd:string |
http://purl.uniprot.org/citations/3311744 | http://purl.uniprot.org/core/author | "Wierenga R.K."xsd:string |
http://purl.uniprot.org/citations/3311744 | http://purl.uniprot.org/core/author | "Opperdoes F.R."xsd:string |
http://purl.uniprot.org/citations/3311744 | http://purl.uniprot.org/core/author | "Lambeir A.M."xsd:string |
http://purl.uniprot.org/citations/3311744 | http://purl.uniprot.org/core/date | "1987"xsd:gYear |
http://purl.uniprot.org/citations/3311744 | http://purl.uniprot.org/core/name | "Eur J Biochem"xsd:string |
http://purl.uniprot.org/citations/3311744 | http://purl.uniprot.org/core/pages | "69-74"xsd:string |
http://purl.uniprot.org/citations/3311744 | http://purl.uniprot.org/core/title | "Kinetic properties of triose-phosphate isomerase from Trypanosoma brucei brucei. A comparison with the rabbit muscle and yeast enzymes."xsd:string |
http://purl.uniprot.org/citations/3311744 | http://purl.uniprot.org/core/volume | "168"xsd:string |
http://purl.uniprot.org/citations/3311744 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/3311744 |
http://purl.uniprot.org/citations/3311744 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/3311744 |
http://purl.uniprot.org/uniprot/#_P00942-mappedCitation-3311744 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/3311744 |
http://purl.uniprot.org/uniprot/P00942 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/3311744 |