| http://purl.uniprot.org/citations/18342615 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/18342615 | http://www.w3.org/2000/01/rdf-schema#comment | "Rat kidney glutamine transaminase K (GTK) exhibits broad specificity both as an aminotransferase and as a cysteine S-conjugate beta-lyase. The beta-lyase reaction products are pyruvate, ammonium and a sulfhydryl-containing fragment. We show here that recombinant human GTK (rhGTK) also exhibits broad specificity both as an aminotransferase and as a cysteine S-conjugate beta-lyase. S-(1,1,2,2-Tetrafluoroethyl)-l-cysteine is an excellent aminotransferase and beta-lyase substrate of rhGTK. Moderate aminotransferase and beta-lyase activities occur with the chemopreventive agent Se-methyl-l-selenocysteine. l-3-(2-Naphthyl)alanine, l-3-(1-naphthyl)alanine, 5-S-l-cysteinyldopamine and 5-S-l-cysteinyl-l-DOPA are measurable aminotransferase substrates, indicating that the active site can accommodate large aromatic amino acids. The alpha-keto acids generated by transamination/l-amino acid oxidase activity of the two catechol cysteine S-conjugates are unstable. A slow rhGTK-catalyzed beta-elimination reaction, as measured by pyruvate formation, was demonstrated with 5-S-l-cysteinyldopamine, but not with 5-S-l-cysteinyl-l-DOPA. The importance of transamination, oxidation and beta-elimination reactions involving 5-S-l-cysteinyldopamine, 5-S-l-cysteinyl-l-DOPA and Se-methyl-l-selenocysteine in human tissues and their biological relevance are discussed."xsd:string |
| http://purl.uniprot.org/citations/18342615 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.abb.2008.02.038"xsd:string |
| http://purl.uniprot.org/citations/18342615 | http://purl.uniprot.org/core/author | "Li J."xsd:string |
| http://purl.uniprot.org/citations/18342615 | http://purl.uniprot.org/core/author | "Spencer J.P."xsd:string |
| http://purl.uniprot.org/citations/18342615 | http://purl.uniprot.org/core/author | "Han Q."xsd:string |
| http://purl.uniprot.org/citations/18342615 | http://purl.uniprot.org/core/author | "Cooper A.J."xsd:string |
| http://purl.uniprot.org/citations/18342615 | http://purl.uniprot.org/core/author | "Pinto J.T."xsd:string |
| http://purl.uniprot.org/citations/18342615 | http://purl.uniprot.org/core/author | "Krasnikov B.F."xsd:string |
| http://purl.uniprot.org/citations/18342615 | http://purl.uniprot.org/core/author | "Vauzour D."xsd:string |
| http://purl.uniprot.org/citations/18342615 | http://purl.uniprot.org/core/author | "Niatsetskaya Z.V."xsd:string |
| http://purl.uniprot.org/citations/18342615 | http://purl.uniprot.org/core/date | "2008"xsd:gYear |
| http://purl.uniprot.org/citations/18342615 | http://purl.uniprot.org/core/name | "Arch Biochem Biophys"xsd:string |
| http://purl.uniprot.org/citations/18342615 | http://purl.uniprot.org/core/pages | "72-81"xsd:string |
| http://purl.uniprot.org/citations/18342615 | http://purl.uniprot.org/core/title | "Substrate specificity of human glutamine transaminase K as an aminotransferase and as a cysteine S-conjugate beta-lyase."xsd:string |
| http://purl.uniprot.org/citations/18342615 | http://purl.uniprot.org/core/volume | "474"xsd:string |
| http://purl.uniprot.org/citations/18342615 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/18342615 |
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