Inhibition of porphobilinogenase by porphyrins in Saccharomyces cerevisiae

The biosynthesis of uroporphyrinogen III, the precursor of hemes, chlorophylls, corrins and related structures, is catalyzed by the porphobilinogenase system (PBGase), a complex of two enzymes, PBG-Deaminase (PBG-D) and Isomerase. Although the separate enzymes have been studied in some detail less w...

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Autores principales:	Araujo, Lidia Susana, Lombardo, María Elisa, Batlle, Alcira María del Carmen
Publicado:	1994
Materias:	Porphobilinogenase Porphyrins Aminolevulinic acid-inhibition Saccharomyces cerevisial Kinetics aminolevulinic acid porphobilinogenase porphyrin unclassified drug article controlled study enzyme inhibition enzyme kinetics nonhuman saccharomyces cerevisiae Aminolevulinic Acid Ammonia-Lyases Kinetics Porphyrins Saccharomyces cerevisiae Support, Non-U.S. Gov't
Acceso en línea:	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_0020711X_v26_n12_p1377_Araujo http://hdl.handle.net/20.500.12110/paper_0020711X_v26_n12_p1377_Araujo
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

id	paper:paper_0020711X_v26_n12_p1377_Araujo
record_format	dspace
spelling	paper:paper_0020711X_v26_n12_p1377_Araujo2023-06-08T14:41:14Z Inhibition of porphobilinogenase by porphyrins in Saccharomyces cerevisiae Araujo, Lidia Susana Lombardo, María Elisa Batlle, Alcira María del Carmen Porphobilinogenase Porphyrins Aminolevulinic acid-inhibition Saccharomyces cerevisial Kinetics aminolevulinic acid porphobilinogenase porphyrin unclassified drug article controlled study enzyme inhibition enzyme kinetics nonhuman saccharomyces cerevisiae Aminolevulinic Acid Ammonia-Lyases Kinetics Porphyrins Saccharomyces cerevisiae Support, Non-U.S. Gov't The biosynthesis of uroporphyrinogen III, the precursor of hemes, chlorophylls, corrins and related structures, is catalyzed by the porphobilinogenase system (PBGase), a complex of two enzymes, PBG-Deaminase (PBG-D) and Isomerase. Although the separate enzymes have been studied in some detail less work has been performed on the properties of the complex. In this study the kinetic behaviour of the enzyme PBGase in a normal yeast strain, D273-10B, and its derivative B231 has been investigated. Uroporphyrinogen formation was linear with time up to 2 hr at 37°C. The enzyme complex shows classical Michaelis-Menten kinetics. From the double reciprocal plots kinetic parameters were estimated for PBGase and PBG-D. Porphyrins were found to be competitive inhibitors with respect to porphobilinogen (PBG) and these compounds appeared to act as inhibitors by forming dead-end complexes with the free enzyme. 5-Aminolevulinic acid (ALA) also inhibited PBGase and this inhibition was overcome by addition of levulinic acid (2μM). These results indicate that ALA, is not an inhibitor but acts through its conversion into porphyrins which are the true inhibitors. © 1994. Fil:Araujo, L.S. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Lombardo, M.E. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Del C. Batlle, A.M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 1994 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_0020711X_v26_n12_p1377_Araujo http://hdl.handle.net/20.500.12110/paper_0020711X_v26_n12_p1377_Araujo
institution	Universidad de Buenos Aires
institution_str	I-28
repository_str	R-134
collection	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic	Porphobilinogenase Porphyrins Aminolevulinic acid-inhibition Saccharomyces cerevisial Kinetics aminolevulinic acid porphobilinogenase porphyrin unclassified drug article controlled study enzyme inhibition enzyme kinetics nonhuman saccharomyces cerevisiae Aminolevulinic Acid Ammonia-Lyases Kinetics Porphyrins Saccharomyces cerevisiae Support, Non-U.S. Gov't
spellingShingle	Porphobilinogenase Porphyrins Aminolevulinic acid-inhibition Saccharomyces cerevisial Kinetics aminolevulinic acid porphobilinogenase porphyrin unclassified drug article controlled study enzyme inhibition enzyme kinetics nonhuman saccharomyces cerevisiae Aminolevulinic Acid Ammonia-Lyases Kinetics Porphyrins Saccharomyces cerevisiae Support, Non-U.S. Gov't Araujo, Lidia Susana Lombardo, María Elisa Batlle, Alcira María del Carmen Inhibition of porphobilinogenase by porphyrins in Saccharomyces cerevisiae
topic_facet	Porphobilinogenase Porphyrins Aminolevulinic acid-inhibition Saccharomyces cerevisial Kinetics aminolevulinic acid porphobilinogenase porphyrin unclassified drug article controlled study enzyme inhibition enzyme kinetics nonhuman saccharomyces cerevisiae Aminolevulinic Acid Ammonia-Lyases Kinetics Porphyrins Saccharomyces cerevisiae Support, Non-U.S. Gov't
description	The biosynthesis of uroporphyrinogen III, the precursor of hemes, chlorophylls, corrins and related structures, is catalyzed by the porphobilinogenase system (PBGase), a complex of two enzymes, PBG-Deaminase (PBG-D) and Isomerase. Although the separate enzymes have been studied in some detail less work has been performed on the properties of the complex. In this study the kinetic behaviour of the enzyme PBGase in a normal yeast strain, D273-10B, and its derivative B231 has been investigated. Uroporphyrinogen formation was linear with time up to 2 hr at 37°C. The enzyme complex shows classical Michaelis-Menten kinetics. From the double reciprocal plots kinetic parameters were estimated for PBGase and PBG-D. Porphyrins were found to be competitive inhibitors with respect to porphobilinogen (PBG) and these compounds appeared to act as inhibitors by forming dead-end complexes with the free enzyme. 5-Aminolevulinic acid (ALA) also inhibited PBGase and this inhibition was overcome by addition of levulinic acid (2μM). These results indicate that ALA, is not an inhibitor but acts through its conversion into porphyrins which are the true inhibitors. © 1994.
author	Araujo, Lidia Susana Lombardo, María Elisa Batlle, Alcira María del Carmen
author_facet	Araujo, Lidia Susana Lombardo, María Elisa Batlle, Alcira María del Carmen
author_sort	Araujo, Lidia Susana
title	Inhibition of porphobilinogenase by porphyrins in Saccharomyces cerevisiae
title_short	Inhibition of porphobilinogenase by porphyrins in Saccharomyces cerevisiae
title_full	Inhibition of porphobilinogenase by porphyrins in Saccharomyces cerevisiae
title_fullStr	Inhibition of porphobilinogenase by porphyrins in Saccharomyces cerevisiae
title_full_unstemmed	Inhibition of porphobilinogenase by porphyrins in Saccharomyces cerevisiae
title_sort	inhibition of porphobilinogenase by porphyrins in saccharomyces cerevisiae
publishDate	1994
url	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_0020711X_v26_n12_p1377_Araujo http://hdl.handle.net/20.500.12110/paper_0020711X_v26_n12_p1377_Araujo
work_keys_str_mv	AT araujolidiasusana inhibitionofporphobilinogenasebyporphyrinsinsaccharomycescerevisiae AT lombardomariaelisa inhibitionofporphobilinogenasebyporphyrinsinsaccharomycescerevisiae AT batllealciramariadelcarmen inhibitionofporphobilinogenasebyporphyrinsinsaccharomycescerevisiae
_version_	1768541782071574528

Inhibition of porphobilinogenase by porphyrins in Saccharomyces cerevisiae

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