Gene Ontology annotation through association of InterPro records with GO terms
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Automatic assignment of GO terms using logical inference, based on on inter-ontology links
TreeGrafter-generated GO annotations
Combined Automated Annotation using Multiple IEA Methods
UniProtKB/Swiss-Prot entry P39051 (TYTR_TRYBB)
Trypanosomes lacking trypanothione reductase are avirulent and show increased sensitivity to oxidative stress.
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Tetracycline-regulated TryR expression in T. brucei shows that less than 10% of wild-type activity blocks growth, causes about 60-fold hypersensitivity to H2O2, and abolishes infectivity in mice.
"trypanosomes containing less than 10% of wild-type enzyme activity were unable to grow, although the levels of reduced trypanothione and total thiols remained constant."
Comparative structural, kinetic and inhibitor studies of Trypanosoma brucei trypanothione reductase with T. cruzi.
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Recombinant T. brucei TryR is a homodimeric FAD flavoprotein (PDB 2WBA) that is highly specific for NADPH and trypanothione disulfide over NADH and glutathione disulfide.
"TbTryR was highly specific for the electron donor (NADPH) and electron acceptor (T(S)2) in the 412 nm assay."
Molecular characterization of the trypanothione reductase gene from Crithidia fasciculata and Trypanosoma brucei: comparison with other flavoprotein disulphide oxidoreductases with respect to substrate specificity and catalytic mechanism.
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Cloning and sequence of the T. brucei TryR gene. TryR belongs to the flavoprotein disulfide oxidoreductase family.
"Trypanothione reductase belongs to the family of flavoprotein disulphide oxidoreductases that include glutathione reductases, dihydrolipoamide dehydrogenases and mercuric reductases."
Trypanothione: a novel bis(glutathionyl)spermidine cofactor for glutathione reductase in trypanosomatids.
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Discovery of trypanothione as the substrate of the trypanosomatid disulfide reductase (then called glutathione reductase).
"Glutathione reductase from trypanosomes and leishmanias, unlike glutathione reductase from other organisms, requires an unusual low molecular weight cofactor for activity."
Metabolism and functions of trypanothione in the Kinetoplastida.
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Review establishing that trypanothione plus TryR replace the GSH/GR system and act in oxidant defense.
"Trypanothione and its related enzymes are involved in defense against damage by oxidants, certain heavy metals, and possibly xenobiotics."
Subcellular distribution of trypanothione reductase in bloodstream and procyclic forms of Trypanosoma brucei.
Targeting trypanothione metabolism in trypanosomatid human parasites.