Purine-specific Nucleoside N-Ribohydrolase from Trypanosoma brucei brucei

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Molecular cloning and expression of a purine-specific N-ribohydrolase from Trypanosoma brucei brucei. Sequence, expression, and molecular analysis.

N-Ribohydrolases, including the inosine-adenosine-guanosine-preferring (IAG) nucleoside hydrolase, have been proposed to be involved in the nucleoside salvage pathway of protozoan parasites and may constitute rational therapeutic targets for the treatment of these diseases. Reported is the complete sequence of the Trypanosoma brucei brucei iagnh gene, which encodes IAG-nucleoside hydrolase. The...

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Trypanosoma brucei brucei

Protein synthesis in Trypanosoma brucei brucei was rapidly inhibited during polyamine depletion by DL-adifluoromethylornithine (DFMO) in vitro and in vivo. [3H]Leucine incorporation was depressed 30-40 % by 24 h and 80-90 % by 48 h of DFMO treatment. Concomitantly there was an apparent decrease in the synthesis of the variant-specific glycoprotein (VSG) in DFMO-treated trypanosomes, as measured...

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Protein isoprenylation in Trypanosoma brucei brucei.

Trypanosoma brucei is a digenetic protozoan parasite presenting a public health hazard in certain areas of Africa; it is transmitted between mammals (bloodstream form (BSF)) by tsetse flies (procyclic form (PCF)). We have an ongoing interest in small GTP proteins in T. brucei, and these are commonly isoprenylated. Many isoprenylated proteins belong to the rab family and include ras; the isopren...

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Structures of adenosine kinase from Trypanosoma brucei brucei.

Trypanosoma brucei is a single-cellular parasite of the genus Kinetoplastida and is the causative agent of African sleeping sickness in humans. Adenosine kinase is a key enzyme in the purine-salvage pathway, phosphorylating adenosine to AMP, and also activates cytotoxic analogues such as cordycepin and Ara-A by their phosphorylation. The structures of T. brucei brucei adenosine kinase (TbAK) in...

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SUMOylation in Trypanosoma brucei

Small ubiquitin like modifier (SUMO) proteins are involved in many processes in eukaryotes. We here show that Trypanosoma brucei SUMO (Tb927.5.3210) modifies many proteins. The levels of SUMOylation were unaffected by temperature changes but were increased by severe oxidative stress. We obtained evidence that trypanosome homologues of the SUMO conjugating enzyme Ubc9 (Tb927.2.2460) and the SUMO...

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ژورنال

عنوان ژورنال: Journal of Biological Chemistry

سال: 1996

ISSN: 0021-9258

DOI: 10.1074/jbc.271.36.21713