Post-translational processing, metabolic stability and catalytic efficiency of oat arginine decarboxylase expressed in Trypanosoma cruzi epimastigotes
Trypanosoma cruzi epimastigotes are auxotrophic for polyamines because they are unable to synthesize putrescine de novo. This deficiency is due to the absence of ornithine and arginine decarboxylase genes in the parasite genome. We have been able to obtain transgenic T. cruzi expressing heterologous...
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2009
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| Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00144894_v122_n3_p169_Serra http://hdl.handle.net/20.500.12110/paper_00144894_v122_n3_p169_Serra |
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paper:paper_00144894_v122_n3_p169_Serra2023-06-08T14:37:23Z Post-translational processing, metabolic stability and catalytic efficiency of oat arginine decarboxylase expressed in Trypanosoma cruzi epimastigotes Serra, María Pía Senn, Alejandro Marcelo Algranati, Israel David α-difluoromethylarginine ADC arginine decarboxylase (EC 4.1.1.9) C-terminal his-tag carbobenzoxyl-leucinyl-leucinyl-leucinal DFMA MG-132 Oat ADC expression ODC ornithine decarboxylase (EC 4.1.1.7) Post-translational processing Protein stability Trypanosoma (Schizotrypanum) cruzi arginine decarboxylase ornithine decarboxylase article carboxy terminal sequence enzyme degradation enzyme stability epimastigote genetic code heterologous expression nonhuman oat priority journal protein cleavage protein expression protein processing Trypanosoma cruzi Amino Acid Sequence Animals Avena sativa Carboxy-Lyases Gene Expression Regulation, Enzymologic Kinetics Molecular Sequence Data Plasmids Protein Processing, Post-Translational Sequence Alignment Transcription, Genetic Trypanosoma cruzi Protozoa Trypanosoma cruzi Trypanosoma cruzi epimastigotes are auxotrophic for polyamines because they are unable to synthesize putrescine de novo. This deficiency is due to the absence of ornithine and arginine decarboxylase genes in the parasite genome. We have been able to obtain transgenic T. cruzi expressing heterologous genes coding for these enzymes. Since arginine decarboxylase normal expression in oat requires a post-translational proteolytic cleavage of an enzyme precursor, we have investigated whether a similar processing occurs inside the transformed protozoa expressing oat arginine decarboxylase or the same enzyme attached to a C-terminal (his)6-tag. We were able to demonstrate that the post-translational processing also takes place inside the transgenic parasites. This cleavage is probably the result of a general proteolytic activity of T. cruzi acting on a protease-sensitive region of the protein. Interestingly, the (his)6-tagged enzyme expressed in the transformed parasites showed considerably increased metabolic stability and catalytic efficiency. © 2008 Elsevier Inc. All rights reserved. Fil:Serra, M.P. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Senn, A.M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Algranati, I.D. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 2009 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00144894_v122_n3_p169_Serra http://hdl.handle.net/20.500.12110/paper_00144894_v122_n3_p169_Serra |
| institution |
Universidad de Buenos Aires |
| institution_str |
I-28 |
| repository_str |
R-134 |
| collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
α-difluoromethylarginine ADC arginine decarboxylase (EC 4.1.1.9) C-terminal his-tag carbobenzoxyl-leucinyl-leucinyl-leucinal DFMA MG-132 Oat ADC expression ODC ornithine decarboxylase (EC 4.1.1.7) Post-translational processing Protein stability Trypanosoma (Schizotrypanum) cruzi arginine decarboxylase ornithine decarboxylase article carboxy terminal sequence enzyme degradation enzyme stability epimastigote genetic code heterologous expression nonhuman oat priority journal protein cleavage protein expression protein processing Trypanosoma cruzi Amino Acid Sequence Animals Avena sativa Carboxy-Lyases Gene Expression Regulation, Enzymologic Kinetics Molecular Sequence Data Plasmids Protein Processing, Post-Translational Sequence Alignment Transcription, Genetic Trypanosoma cruzi Protozoa Trypanosoma cruzi |
| spellingShingle |
α-difluoromethylarginine ADC arginine decarboxylase (EC 4.1.1.9) C-terminal his-tag carbobenzoxyl-leucinyl-leucinyl-leucinal DFMA MG-132 Oat ADC expression ODC ornithine decarboxylase (EC 4.1.1.7) Post-translational processing Protein stability Trypanosoma (Schizotrypanum) cruzi arginine decarboxylase ornithine decarboxylase article carboxy terminal sequence enzyme degradation enzyme stability epimastigote genetic code heterologous expression nonhuman oat priority journal protein cleavage protein expression protein processing Trypanosoma cruzi Amino Acid Sequence Animals Avena sativa Carboxy-Lyases Gene Expression Regulation, Enzymologic Kinetics Molecular Sequence Data Plasmids Protein Processing, Post-Translational Sequence Alignment Transcription, Genetic Trypanosoma cruzi Protozoa Trypanosoma cruzi Serra, María Pía Senn, Alejandro Marcelo Algranati, Israel David Post-translational processing, metabolic stability and catalytic efficiency of oat arginine decarboxylase expressed in Trypanosoma cruzi epimastigotes |
| topic_facet |
α-difluoromethylarginine ADC arginine decarboxylase (EC 4.1.1.9) C-terminal his-tag carbobenzoxyl-leucinyl-leucinyl-leucinal DFMA MG-132 Oat ADC expression ODC ornithine decarboxylase (EC 4.1.1.7) Post-translational processing Protein stability Trypanosoma (Schizotrypanum) cruzi arginine decarboxylase ornithine decarboxylase article carboxy terminal sequence enzyme degradation enzyme stability epimastigote genetic code heterologous expression nonhuman oat priority journal protein cleavage protein expression protein processing Trypanosoma cruzi Amino Acid Sequence Animals Avena sativa Carboxy-Lyases Gene Expression Regulation, Enzymologic Kinetics Molecular Sequence Data Plasmids Protein Processing, Post-Translational Sequence Alignment Transcription, Genetic Trypanosoma cruzi Protozoa Trypanosoma cruzi |
| description |
Trypanosoma cruzi epimastigotes are auxotrophic for polyamines because they are unable to synthesize putrescine de novo. This deficiency is due to the absence of ornithine and arginine decarboxylase genes in the parasite genome. We have been able to obtain transgenic T. cruzi expressing heterologous genes coding for these enzymes. Since arginine decarboxylase normal expression in oat requires a post-translational proteolytic cleavage of an enzyme precursor, we have investigated whether a similar processing occurs inside the transformed protozoa expressing oat arginine decarboxylase or the same enzyme attached to a C-terminal (his)6-tag. We were able to demonstrate that the post-translational processing also takes place inside the transgenic parasites. This cleavage is probably the result of a general proteolytic activity of T. cruzi acting on a protease-sensitive region of the protein. Interestingly, the (his)6-tagged enzyme expressed in the transformed parasites showed considerably increased metabolic stability and catalytic efficiency. © 2008 Elsevier Inc. All rights reserved. |
| author |
Serra, María Pía Senn, Alejandro Marcelo Algranati, Israel David |
| author_facet |
Serra, María Pía Senn, Alejandro Marcelo Algranati, Israel David |
| author_sort |
Serra, María Pía |
| title |
Post-translational processing, metabolic stability and catalytic efficiency of oat arginine decarboxylase expressed in Trypanosoma cruzi epimastigotes |
| title_short |
Post-translational processing, metabolic stability and catalytic efficiency of oat arginine decarboxylase expressed in Trypanosoma cruzi epimastigotes |
| title_full |
Post-translational processing, metabolic stability and catalytic efficiency of oat arginine decarboxylase expressed in Trypanosoma cruzi epimastigotes |
| title_fullStr |
Post-translational processing, metabolic stability and catalytic efficiency of oat arginine decarboxylase expressed in Trypanosoma cruzi epimastigotes |
| title_full_unstemmed |
Post-translational processing, metabolic stability and catalytic efficiency of oat arginine decarboxylase expressed in Trypanosoma cruzi epimastigotes |
| title_sort |
post-translational processing, metabolic stability and catalytic efficiency of oat arginine decarboxylase expressed in trypanosoma cruzi epimastigotes |
| publishDate |
2009 |
| url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00144894_v122_n3_p169_Serra http://hdl.handle.net/20.500.12110/paper_00144894_v122_n3_p169_Serra |
| work_keys_str_mv |
AT serramariapia posttranslationalprocessingmetabolicstabilityandcatalyticefficiencyofoatargininedecarboxylaseexpressedintrypanosomacruziepimastigotes AT sennalejandromarcelo posttranslationalprocessingmetabolicstabilityandcatalyticefficiencyofoatargininedecarboxylaseexpressedintrypanosomacruziepimastigotes AT algranatiisraeldavid posttranslationalprocessingmetabolicstabilityandcatalyticefficiencyofoatargininedecarboxylaseexpressedintrypanosomacruziepimastigotes |
| _version_ |
1768544115550584832 |