http://purl.uniprot.org/citations/18522537 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/18522537 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/18522537 | http://www.w3.org/2000/01/rdf-schema#comment | "TbTDPX (Trypanosoma brucei tryparedoxin-dependent peroxidase) is a genetically validated drug target in the fight against African sleeping sickness. Despite its similarity to members of the GPX (glutathione peroxidase) family, TbTDPX2 is functional as a monomer, lacks a selenocysteine residue and relies instead on peroxidatic and resolving cysteine residues for catalysis and uses tryparedoxin rather than glutathione as electron donor. Kinetic studies indicate a saturable Ping Pong mechanism, unlike selenium-dependent GPXs, which display infinite K(m) and V(max) values. The structure of the reduced enzyme at 2.1 A (0.21 nm) resolution reveals that the catalytic thiol groups are widely separated [19 A (0.19 nm)] and thus unable to form a disulphide bond without a large conformational change in the secondary-structure architecture, as reported for certain plant GPXs. A model of the oxidized enzyme structure is presented and the implications for small-molecule inhibition are discussed."xsd:string |
http://purl.uniprot.org/citations/18522537 | http://purl.org/dc/terms/identifier | "doi:10.1042/BJ20080889"xsd:string |
http://purl.uniprot.org/citations/18522537 | http://purl.org/dc/terms/identifier | "doi:10.1042/bj20080889"xsd:string |
http://purl.uniprot.org/citations/18522537 | http://purl.uniprot.org/core/author | "Fairlamb A.H."xsd:string |
http://purl.uniprot.org/citations/18522537 | http://purl.uniprot.org/core/author | "Fairlamb A.H."xsd:string |
http://purl.uniprot.org/citations/18522537 | http://purl.uniprot.org/core/author | "Alphey M.S."xsd:string |
http://purl.uniprot.org/citations/18522537 | http://purl.uniprot.org/core/author | "Alphey M.S."xsd:string |
http://purl.uniprot.org/citations/18522537 | http://purl.uniprot.org/core/author | "Konig J."xsd:string |
http://purl.uniprot.org/citations/18522537 | http://purl.uniprot.org/core/author | "Konig J."xsd:string |
http://purl.uniprot.org/citations/18522537 | http://purl.uniprot.org/core/date | "2008"xsd:gYear |
http://purl.uniprot.org/citations/18522537 | http://purl.uniprot.org/core/date | "2008"xsd:gYear |
http://purl.uniprot.org/citations/18522537 | http://purl.uniprot.org/core/name | "Biochem. J."xsd:string |
http://purl.uniprot.org/citations/18522537 | http://purl.uniprot.org/core/name | "Biochem J"xsd:string |
http://purl.uniprot.org/citations/18522537 | http://purl.uniprot.org/core/pages | "375-381"xsd:string |
http://purl.uniprot.org/citations/18522537 | http://purl.uniprot.org/core/pages | "375-381"xsd:string |
http://purl.uniprot.org/citations/18522537 | http://purl.uniprot.org/core/title | "Structural and mechanistic insights into type II trypanosomatid tryparedoxin-dependent peroxidases."xsd:string |
http://purl.uniprot.org/citations/18522537 | http://purl.uniprot.org/core/title | "Structural and mechanistic insights into type II trypanosomatid tryparedoxin-dependent peroxidases."xsd:string |
http://purl.uniprot.org/citations/18522537 | http://purl.uniprot.org/core/volume | "414"xsd:string |
http://purl.uniprot.org/citations/18522537 | http://purl.uniprot.org/core/volume | "414"xsd:string |
http://purl.uniprot.org/citations/18522537 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/18522537 |
http://purl.uniprot.org/citations/18522537 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/18522537 |
http://purl.uniprot.org/citations/18522537 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/18522537 |
http://purl.uniprot.org/citations/18522537 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/18522537 |