Studies on uroporphyrinogen decarboxylase from Chlorella kessleri (Trebouxiophyceae, Chlorophyta)
Uroporphyrinogen decarboxylase (UroD) (EC 4.1.1.37) is an enzyme from the tetrapyrrole biosynthetic pathway, in which chlorophyll is the main final product in algae. This is the first time that a study on UroD activity has been performed in a green alga (Chlorella). We isolated and partially purifie...
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Acceso en línea: | https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00084166_v53_n2_p303_Juarez http://hdl.handle.net/20.500.12110/paper_00084166_v53_n2_p303_Juarez |
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paper:paper_00084166_v53_n2_p303_Juarez2023-06-08T14:31:59Z Studies on uroporphyrinogen decarboxylase from Chlorella kessleri (Trebouxiophyceae, Chlorophyta) Juárez, Angela Beatriz Vigna, María Susana Ríos de Molina, María del Carmen Chlorella kessleri Chlorophyll Chlorophyta Porphyrins Uroporphyrinogen decarboxylase Bioassay Biosynthesis Chlorophyll Chromatographic analysis Molecular mass Porphyrins Reaction kinetics Biosynthetic pathway Chlorella kessleri Chlorophyta Decarboxylation Enzyme kinetics chlorophyll uroporphyrinogen decarboxylase alga bioassay decarboxylation enzyme activity growth rate porphyrin article Chlorella controlled study decarboxylation enzyme activity enzyme purification gel filtration green alga incubation time nonhuman priority journal Western blotting Chlorella Molecular Weight Uroporphyrinogen Decarboxylase algae Chlorella (Chlorellales) Chlorella (Prasiolales) Chlorella (unclassified Chlorophyceae) Chlorella (unclassified Trebouxiophyceae) Chlorophyta Parachlorella kessleri Trebouxiophyceae Uroporphyrinogen decarboxylase (UroD) (EC 4.1.1.37) is an enzyme from the tetrapyrrole biosynthetic pathway, in which chlorophyll is the main final product in algae. This is the first time that a study on UroD activity has been performed in a green alga (Chlorella). We isolated and partially purified the enzyme from a Chlorella kessleri (Trebouxiophyceae, Chlorophyta) strain (Copahue, Neuquen, Argentina), and describe for the first time some of its properties. In C. kessleri, the decarboxylation of uroporphyrinogen III occurs in two stages, via 7 COOH and then 6 and 5 COOH intermediates, with the decarboxylation of the 7 COOH compound being the rate-limiting step for the reaction. Cultures in the exponential growth phase showed the highest specific activity values. The most suitable conditions to measure UroD activity in C. kessleri were as follows: 0.23-0.3 mg protein/mL, ≈6-8 μmol/L uroporphyrinogen III, and 20 min incubation time. Gel filtration chromatography and Western blot assays indicated that UroD from C. kessleri is a dimer of approximately 90 kDa formed by species of lower molecular mass, which conserves enzymatic activity. © 2007 NRC. Fil:Juárez, A.B. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Vigna, M.S. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Ríos De Molina, M.C. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 2007 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00084166_v53_n2_p303_Juarez http://hdl.handle.net/20.500.12110/paper_00084166_v53_n2_p303_Juarez |
institution |
Universidad de Buenos Aires |
institution_str |
I-28 |
repository_str |
R-134 |
collection |
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
topic |
Chlorella kessleri Chlorophyll Chlorophyta Porphyrins Uroporphyrinogen decarboxylase Bioassay Biosynthesis Chlorophyll Chromatographic analysis Molecular mass Porphyrins Reaction kinetics Biosynthetic pathway Chlorella kessleri Chlorophyta Decarboxylation Enzyme kinetics chlorophyll uroporphyrinogen decarboxylase alga bioassay decarboxylation enzyme activity growth rate porphyrin article Chlorella controlled study decarboxylation enzyme activity enzyme purification gel filtration green alga incubation time nonhuman priority journal Western blotting Chlorella Molecular Weight Uroporphyrinogen Decarboxylase algae Chlorella (Chlorellales) Chlorella (Prasiolales) Chlorella (unclassified Chlorophyceae) Chlorella (unclassified Trebouxiophyceae) Chlorophyta Parachlorella kessleri Trebouxiophyceae |
spellingShingle |
Chlorella kessleri Chlorophyll Chlorophyta Porphyrins Uroporphyrinogen decarboxylase Bioassay Biosynthesis Chlorophyll Chromatographic analysis Molecular mass Porphyrins Reaction kinetics Biosynthetic pathway Chlorella kessleri Chlorophyta Decarboxylation Enzyme kinetics chlorophyll uroporphyrinogen decarboxylase alga bioassay decarboxylation enzyme activity growth rate porphyrin article Chlorella controlled study decarboxylation enzyme activity enzyme purification gel filtration green alga incubation time nonhuman priority journal Western blotting Chlorella Molecular Weight Uroporphyrinogen Decarboxylase algae Chlorella (Chlorellales) Chlorella (Prasiolales) Chlorella (unclassified Chlorophyceae) Chlorella (unclassified Trebouxiophyceae) Chlorophyta Parachlorella kessleri Trebouxiophyceae Juárez, Angela Beatriz Vigna, María Susana Ríos de Molina, María del Carmen Studies on uroporphyrinogen decarboxylase from Chlorella kessleri (Trebouxiophyceae, Chlorophyta) |
topic_facet |
Chlorella kessleri Chlorophyll Chlorophyta Porphyrins Uroporphyrinogen decarboxylase Bioassay Biosynthesis Chlorophyll Chromatographic analysis Molecular mass Porphyrins Reaction kinetics Biosynthetic pathway Chlorella kessleri Chlorophyta Decarboxylation Enzyme kinetics chlorophyll uroporphyrinogen decarboxylase alga bioassay decarboxylation enzyme activity growth rate porphyrin article Chlorella controlled study decarboxylation enzyme activity enzyme purification gel filtration green alga incubation time nonhuman priority journal Western blotting Chlorella Molecular Weight Uroporphyrinogen Decarboxylase algae Chlorella (Chlorellales) Chlorella (Prasiolales) Chlorella (unclassified Chlorophyceae) Chlorella (unclassified Trebouxiophyceae) Chlorophyta Parachlorella kessleri Trebouxiophyceae |
description |
Uroporphyrinogen decarboxylase (UroD) (EC 4.1.1.37) is an enzyme from the tetrapyrrole biosynthetic pathway, in which chlorophyll is the main final product in algae. This is the first time that a study on UroD activity has been performed in a green alga (Chlorella). We isolated and partially purified the enzyme from a Chlorella kessleri (Trebouxiophyceae, Chlorophyta) strain (Copahue, Neuquen, Argentina), and describe for the first time some of its properties. In C. kessleri, the decarboxylation of uroporphyrinogen III occurs in two stages, via 7 COOH and then 6 and 5 COOH intermediates, with the decarboxylation of the 7 COOH compound being the rate-limiting step for the reaction. Cultures in the exponential growth phase showed the highest specific activity values. The most suitable conditions to measure UroD activity in C. kessleri were as follows: 0.23-0.3 mg protein/mL, ≈6-8 μmol/L uroporphyrinogen III, and 20 min incubation time. Gel filtration chromatography and Western blot assays indicated that UroD from C. kessleri is a dimer of approximately 90 kDa formed by species of lower molecular mass, which conserves enzymatic activity. © 2007 NRC. |
author |
Juárez, Angela Beatriz Vigna, María Susana Ríos de Molina, María del Carmen |
author_facet |
Juárez, Angela Beatriz Vigna, María Susana Ríos de Molina, María del Carmen |
author_sort |
Juárez, Angela Beatriz |
title |
Studies on uroporphyrinogen decarboxylase from Chlorella kessleri (Trebouxiophyceae, Chlorophyta) |
title_short |
Studies on uroporphyrinogen decarboxylase from Chlorella kessleri (Trebouxiophyceae, Chlorophyta) |
title_full |
Studies on uroporphyrinogen decarboxylase from Chlorella kessleri (Trebouxiophyceae, Chlorophyta) |
title_fullStr |
Studies on uroporphyrinogen decarboxylase from Chlorella kessleri (Trebouxiophyceae, Chlorophyta) |
title_full_unstemmed |
Studies on uroporphyrinogen decarboxylase from Chlorella kessleri (Trebouxiophyceae, Chlorophyta) |
title_sort |
studies on uroporphyrinogen decarboxylase from chlorella kessleri (trebouxiophyceae, chlorophyta) |
publishDate |
2007 |
url |
https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_00084166_v53_n2_p303_Juarez http://hdl.handle.net/20.500.12110/paper_00084166_v53_n2_p303_Juarez |
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